Book
1 online resource.
  • Employing 'second generation' matrices.- (MA)LDI MS mass spectrometry imaging at high specificity and sensitivity.- Techniques for fingermark analysis using MALDI MS - a practical overview.- Whole/Intact Cell MALDI MS Biotyping in Mammalian Cell Analyis.- MALDI biotyping for microorganism identification in clinical microbiology.- Future applications of MALDI-TOF MS in microbiology.- MALDESI: Fundamentals, direct analysis, and MS imaging.- Microprobe MS Imaging of Live Tissues, Cells, and Bacterial Colonies using LAESI.- Efficient production of multiply charged MALDI ions.- Food Authentication by MALDI MS - MALDI-TOF MS Analysis of Fish Species.- Quantitative MALDI MS using Ionic Liquid Matrices.- Disease profiling by MALDI MS analysis of biofluids.- Ionic Liquids and other liquid matrices for sensitive MALDI MS analysis.- Coupling liquid MALDI MS to liquid chromatography.
  • (source: Nielsen Book Data)9783319048185 20160619
This book covers the state-of-the-art of modern MALDI (matrix-assisted laser desorption/ionization) and its applications. New applications and improvements in the MALDI field such as biotyping, clinical diagnosis, forensic imaging, and ESI-like ion production are covered in detail. Additional topics include MS imaging, biotyping/speciation and large-scale, high-speed MS sample profiling, new methods based on MALDI or MALDI-like sample preparations, and the advantages of ESI to MALDI MS analysis. This is an ideal book for graduate students and researchers in the field of bioanalytical sciences. This book also: * Showcases new techniques and applications in MALDI MS * Demonstrates how MALDI is preferable to ESI (electrospray ionization) * Illustrates the pros and cons associated with biomarker discovery studies in clinical proteomics and the various application areas, such as cancer proteomics.
(source: Nielsen Book Data)9783319048185 20160619
Book
xii, 269 pages : illustrations, map ; 24 cm
  • Principles and applications of ion chromatography / Rajmund Michalski
  • Mass spectrometric detectors for environmental studies / Maria Balcerzak
  • High-performance liquid chromatography coupled to inductively coupled plasma MS/electrospray ionization MS / Jürgen Mattusch
  • Application of IC-MS in organic environmental geochemistry / Klaus Fischer
  • Analysis of oxyhalides and haloacetic acids in drinking water using IC-MS and IC-ICP-MS / Koji Kosaka
  • Analysis of various anionic metabolites in plant and animal material by IC-MS / Adam Konrad Jagielski and Michal Usarek
  • Analysis of perchlorate ion in various matrices using ion chromatography hyphenated with mass spectrometry / Jay Gandhi
  • Sample preparation techniques for ion chromatography / Wolfgang Frenzel and Rajmund Michalski.
Biology Library (Falconer)
Book
1 online resource (viii, 336 pages) : illustrations (some color)
In the last quarter century, advances in mass spectrometry (MS) have been at the forefront of efforts to map complex biological systems including the human metabolome, proteome, and microbiome. All of these developments have allowed MS to become a well-established molecular level technology for microbial characterization. MS has demonstrated its considerable advantage as a rapid, accurate, and cost-effective method for microbial identification, compared to conventional phenotypic techniques. In the last several years, applications of MS for microbial characterization in research, clinical microbiology, counter-bioterrorism, food safety, and environmental monitoring have been documented in thousands of publications. Regulatory bodies in Europe, the US, and elsewhere have approved MS-based assays for infectious disease diagnostics. As of mid-2015, more than 3300 commercial MS systems for microbial identification have been deployed worldwide in hospitals and clinical labs. While previous work has covered broader approaches in using MS to characterize microorganisms at the species level or above, this book focuses on strain-level and subtyping applications. In thirteen individual chapters, innovators, leaders and practitioners in the field from around the world have contributed to a comprehensive overview of current and next-generation approaches for MS-based microbial characterization at the subspecies and strain levels. Chapters include up-to-date reference lists as well as web-links to databases, recommended software, and other useful tools. The emergence of new, antibiotic-resistant strains of human or animal pathogens is of extraordinary concern not only to the scientific and medical communities, but to the general public as well. Developments of novel MS-based assays for rapid identification of strains of antibiotic-resistant microorganisms are reviewed in the book as well. Microbiologists, bioanalytical scientists, infectious disease specialists, clinical laboratory and public health practitioners as well as researchers in universities, hospitals, government labs, and the pharmaceutical and biotechnology industries will find this book to be a timely and valuable resource.
Book
1 online resource (Article No. 22321 ) : digital, PDF file.
In this study, we report the atomic-scale analysis of biological interfaces using atom probe tomography. Embedding the protein ferritin in an organic polymer resin lacking nitrogen provided chemical contrast to visualize atomic distributions and distinguish organic-organic and organic-inorganic interfaces. The sample preparation method can be directly extended to further enhance the study of biological, organic and inorganic nanomaterials relevant to health, energy or the environment.
Collection
Undergraduate Theses, Department of Biology, 2015-2016
Population growth places great strain on our natural resources, bringing to the forefront the pressing problems such as limited food supplies. One way to address this problem is by improving plant photosynthetic efficiency, resulting in increased plant productivity and higher crop yields. To study photosynthesis and carbon concentration, we use the model organism Chlamydomonas reinhardtii, a single-celled green alga with an inducible carbon concentrating mechanism (CCM) that allows it to perform efficient photosynthesis: our long-term goal is to introduce the algal CCM into higher land plants, which would reduce photorespiration and enhance photosynthesis. It is necessary, therefore, to identify the key components of the CCM and to understand their molecular interactions in order to transfer this mechanism into crop plants. To this end, we have developed a pipeline for large-scale characterization of the algal CCM components and map how these components function together. With fluorescent and affinity tagging coupled to immunoprecipitation (IP) and mass spectrometry to explore these mechanisms, we took the localization data for 40 putative photosynthesis and CCM components to present 381 confident interactions between the proteins involved. The developed pipeline and the foundational knowledge reported here provide valuable tools for continuing work towards bioengineering of the CCM.
Book
online resource (xv, 333 pages) : illustrations (some color)
  • Mass spectrometry in clinical laboratory : applications in biomolecular analysis / Uttam Garg and Yan Victoria Zhang
  • Quantification of free carnitine and acylcarnitines in plasma or serum using HPLC/MS/MS / David Scott, Bryce Heese, and Uttam Garg
  • Quantification of arginine and its methylated derivatives in plasma by high-performance liquid chromatography tandem mass spectrometry (LC-MS/MS) / Faye B. Vicente ... [et al.]
  • Quantitation of albumin in urine by liquid chromatography tandem mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Quantitation of aldosterone in serum or plasma using liquid chromatography-tandem mass spectrometry (LC- MS/MS) / J. Grace Van Der Gugten and Daniel T. Holmes
  • Quantification of five clinically important amino acids by HPLC-Triple TOF 5600 based on pre-column double derivatization method / Shuang Deng, David Scott, and Uttam Garg
  • Sensitive, simple, and robust nano-liquid chromatography-mass spectrometry method for amyloid protein subtyping / Drew Payto, Courtney Heideloff, and Sihe Wang
  • Quantitation of ubiquinone (coenzyme Q10) in serum/plasma using liquid chromatography electrospray tandem mass spectrometry (ESI-LC-MS/MS) / Richard E. Mathieu Jr. and Catherine P. Riley
  • Quantitative analysis of salivary cortisol using LC-MS/MS / Yan Victoria Zhang
  • Quantification of dihydroxyacetone phosphate (DHAP) in human red blood cells by HPLC-TripleTOF 5600 mass spectrometer / Shuang Deng ... [et al.]
  • Simultaneous quantitation of estradiol and sstrone in serum using liquid chromatography mass spectrometry / Catherine P. Riley, Richard E. Mathieu Jr., and Carmen Wiley
  • Direct measurement of free estradiol in human serum and plasma by equilibrium dialysis-liquid chromatography-tandem mass spectrometry / Julie A. Ray ... [et al.]
  • Quantification of γ-aminobutyric acid in cerebrospinal fluid using liquid chromatography-electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Quantitation of insulin analogues in serum using immunoaffinity extraction, liquid chromatography, and tandem mass spectrometry / J. Grace Van Der Gugten, Sophia Wong, and Daniel T. Holmes
  • Quantitation of insulin-like growth factor 1 in serum by liquid chromatography high resolution accurate-mass mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Quantitation of free metanephrines in plasma by liquid chromatography-tandem mass spectrometry / Courtney Heideloff, Drew Payto, and Sihe Wang
  • Quantification of metanephrine and normetanephrine in urine using liquid chromatography-tandem mass spectrometry / Jessica Gabler and Sihe Wang
  • High-throughput analysis of methylmalonic acid in serum, plasma, and urine by LC-MS/MS. Method for analyzing isomers without chromatographic separation / Mark M. Kushnir ... [et al.]
  • Quantitation of 5-methyltetrahydrofolate in cerebrospinal fluid using liquid chromatography-electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Quantitative organic acids in urine by two dimensional gas chromatography-time of flight mass spectrometry (GCxGC-TOFMS) / Lawrence Sweetman, Paula Ashcraft, and Jeanna Bennett-Firmin
  • High sensitivity measurement of pancreatic polypeptide and its variant in serum and plasma by LC-MS/MS / Hernando Escobar ... [et al.]
  • Quantitation of parathyroid hormone in serum or plasma by liquid chromatography-tandem mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Determination of phenylalanine and tyrosine by high performance liquid chromatography-tandem mass spectrometry / Judy Peat and Uttam Garg
  • Urine purine metabolite determination by UPLC-tandem mass spectrometry / Qin Sun
  • Urine pyrimidine metabolite determination by HPLC tandem mass spectrometry / Qin Sun
  • Quantitation of plasma renin activity in plasma using liquid chromatography-tandem mass spectrometry (LC- MS/MS) / J. Grace Van Der Gugten and Daniel T. Holmes
  • Quantitation of S-adenosylmethionine and S-adenosylhomocysteine in plasma using liquid chromatography electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Simple, high-throughput method for analysis of ceramide, glucosylceramide, and ceramide trihexoside in dried blood spots by LC/MS/MS / Wei-Lien Chuang, Joshua Pacheco, and Kate Zhang
  • Quantification of dehydroepiandrosterone, 11-Deoxycortisol, 17-Hydroxyprogesterone, and testosterone by liquid chromatography-tandem mass spectrometry (LC/MS/MS) / Ada Munar, Clint Frazee, and Uttam Garg
  • Urinary succinylacetone analysis by gas chromatography-mass spectrometry (GC-MS) / Hongjie Chen and Chunli Yu
  • Quantification of 1,25-Dihydroxyvitamin D2 and D3 in serum using liquid chromatography-tandem mass spectrometry / Jonathon Mahlow, Dustin R. Bunch, and Sihe Wang
  • High-throughput serum 25-hydroxy vitamin D testing with automated sample preparation / Judy Stone
  • Quantitation of 25-OH-Vitamin-D2 and 25-OH-Vitamin-D3 in urine using LC-MS/MS / Dean C. Carlow, Ryan C. Schofield, and Michelle Denburg.
Medical Library (Lane)
Book
xv, 333 pages : illustrations (some color) ; 26 cm.
  • Mass spectrometry in clinical laboratory : applications in biomolecular analysis / Uttam Garg and Yan Victoria Zhang
  • Quantification of free carnitine and acylcarnitines in plasma or serum using HPLC/MS/MS / David Scott, Bryce Heese, and Uttam Garg
  • Quantification of arginine and its methylated derivatives in plasma by high-performance liquid chromatography tandem mass spectrometry (LC-MS/MS) / Faye B. Vicente [and others]
  • Quantitation of albumin in urine by liquid chromatography tandem mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Quantitation of aldosterone in serum or plasma using liquid chromatography-tandem mass spectrometry (LC- MS/MS) / J. Grace Van Der Gugten and Daniel T. Holmes
  • Quantification of five clinically important amino acids by HPLC-Triple TOF 5600 based on pre-column double derivatization method / Shuang Deng, David Scott, and Uttam Garg
  • Sensitive, simple, and robust nano-liquid chromatography-mass spectrometry method for amyloid protein subtyping / Drew Payto, Courtney Heideloff, and Sihe Wang
  • Quantitation of ubiquinone (coenzyme Q10) in serum/plasma using liquid chromatography electrospray tandem mass spectrometry (ESI-LC-MS/MS) / Richard E. Mathieu Jr. and Catherine P. Riley
  • Quantitative analysis of salivary cortisol using LC-MS/MS / Yan Victoria Zhang
  • Quantification of dihydroxyacetone phosphate (DHAP) in human red blood cells by HPLC-TripleTOF 5600 mass spectrometer / Shuang Deng [and others]
  • Simultaneous quantitation of estradiol and sstrone in serum using liquid chromatography mass spectrometry / Catherine P. Riley, Richard E. Mathieu Jr., and Carmen Wiley
  • Direct measurement of free estradiol in human serum and plasma by equilibrium dialysis-liquid chromatography-tandem mass spectrometry / Julie A. Ray [and others]
  • Quantification of γ-aminobutyric acid in cerebrospinal fluid using liquid chromatography-electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Quantitation of insulin analogues in serum using immunoaffinity extraction, liquid chromatography, and tandem mass spectrometry / J. Grace Van Der Gugten, Sophia Wong, and Daniel T. Holmes
  • Quantitation of insulin-like growth factor 1 in serum by liquid chromatography high resolution accurate-mass mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Quantitation of free metanephrines in plasma by liquid chromatography-tandem mass spectrometry / Courtney Heideloff, Drew Payto, and Sihe Wang
  • Quantification of metanephrine and normetanephrine in urine using liquid chromatography-tandem mass spectrometry / Jessica Gabler and Sihe Wang
  • High-throughput analysis of methylmalonic acid in serum, plasma, and urine by LC-MS/MS. Method for analyzing isomers without chromatographic separation / Mark M. Kushnir [and others]
  • Quantitation of 5-methyltetrahydrofolate in cerebrospinal fluid using liquid chromatography-electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Quantitative organic acids in urine by two dimensional gas chromatography-time of flight mass spectrometry (GCxGC-TOFMS) / Lawrence Sweetman, Paula Ashcraft, and Jeanna Bennett-Firmin
  • High sensitivity measurement of pancreatic polypeptide and its variant in serum and plasma by LC-MS/MS / Hernando Escobar [and others]
  • Quantitation of parathyroid hormone in serum or plasma by liquid chromatography-tandem mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Determination of phenylalanine and tyrosine by high performance liquid chromatography-tandem mass spectrometry / Judy Peat and Uttam Garg
  • Urine purine metabolite determination by UPLC-tandem mass spectrometry / Qin Sun
  • Urine pyrimidine metabolite determination by HPLC tandem mass spectrometry / Qin Sun
  • Quantitation of plasma renin activity in plasma using liquid chromatography-tandem mass spectrometry (LC- MS/MS) / J. Grace Van Der Gugten and Daniel T. Holmes
  • Quantitation of S-adenosylmethionine and S-adenosylhomocysteine in plasma using liquid chromatography electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Simple, high-throughput method for analysis of ceramide, glucosylceramide, and ceramide trihexoside in dried blood spots by LC/MS/MS / Wei-Lien Chuang, Joshua Pacheco, and Kate Zhang
  • Quantification of dehydroepiandrosterone, 11-Deoxycortisol, 17-Hydroxyprogesterone, and testosterone by liquid chromatography-tandem mass spectrometry (LC/MS/MS) / Ada Munar, Clint Frazee, and Uttam Garg
  • Urinary succinylacetone analysis by gas chromatography-mass spectrometry (GC-MS) / Hongjie Chen and Chunli Yu
  • Quantification of 1,25-Dihydroxyvitamin D2 and D3 in serum using liquid chromatography-tandem mass spectrometry / Jonathon Mahlow, Dustin R. Bunch, and Sihe Wang
  • High-throughput serum 25-hydroxy vitamin D testing with automated sample preparation / Judy Stone
  • Quantitation of 25-OH-Vitamin-D2 and 25-OH-Vitamin-D3 in urine using LC-MS/MS / Dean C. Carlow, Ryan C. Schofield, and Michelle Denburg.
This volume provides stepwise instructions for the analysis of numerous clinically important analytes by mass spectrometry. Mass spectrometry offers clinical laboratory scientists a number of advantages including increased sensitivity and specificity, multiple component analysis, and no need for specialized reagents. The techniques described are a must for the measurement of many clinically relevant analytes in the fields of drug analysis, endocrinology, and inborn errors of metabolism. Each chapter provides a brief introduction about a specified analyte, followed by detailed instructions on the analytical protocol. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Cutting edge and practical, Clinical Applications of Mass Spectrometry in Biomolecular Analysis: Methods and Protocols is a great resource for clinical laboratory scientists who are already using or thinking of bringing mass spectrometry to their laboratories.
(source: Nielsen Book Data)9781493931811 20160619
Biology Library (Falconer)
Book
xv, 272 pages : illustrations (some color) ; 26 cm.
  • Mass spectrometry in clinical laboratory : applications in therapeutic drug monitoring and toxicology / Uttam Garg and Yan Victoria Zhang
  • Quantitation of flecainide, mexiletine, propafenone, and amiodarone in serum or plasma using liquid chromatography-tandem mass spectrometry (LC-MS/MS) / Matthew H. Slawson and Kamisha L. Johnson-Davis
  • Quantitation of the oral anticoagulants dabigatran, rivaroxaban, apixaban, and warfarin in plasma using ultra-performance liquid chromatography with tandem mass spectrometry (UPLC-MS/MS) / Jaime H. Noguez and James C. Ritchie
  • Simultaneous quantitation of lamotrigine, levetiracetam, 10-Hydroxycarbazepine, topiramate, and zonisamide in serum using HPLC-MS/MS / Dean C. Carlow, Heng Shi, and Ryan C. Schofield
  • Quantification of the triazole antifungal compounds voriconazole and posaconazole in human serum or plasma using liquid chromatography electrospray tandem mass spectrometry (HPLC-ESI-MS/MS) / Alejandro R. Molinelli and Charles H. Rose IV
  • Quantitation of haloperidol, fluphenazine, perphenazine, and thiothixene in serum or plasma using liquid chromatography-tandem mass spectrometry (LC-MS/MS) / Matthew H. Slawson and Kamisha L. Johnson-Davis
  • Quantitation of total buprenorphine and norbuprenorphine in meconium by LC-MS/MS / Stephanie J. Marin and Gwendolyn A. McMillin
  • Quantitation of buprenorphine, norbuprenorphine, buprenorphine glucuronide, norbuprenorphine glucuronide, and naloxone in urine by LC-MS/MS / Stephanie J. Marin and Gwendolyn A. McMillin
  • Simple liquid chromatography tandem mass spectrometry method for quantitation of plasma busulfan / Shuang Deng [and others]
  • High-throughput quantitation of busulfan in plasma using ultrafast solid-phase extraction tandem mass spectrometry (SPE-MS/MS) / Loralie J. Langman [and others]
  • Quantification of 11-carboxy-delta-9-tetrahydrocannabinol (THC-COOH) in meconium using gas chromatography/mass spectrometry (GC/MS) / Judy Peat [and others]
  • Quantitation of carisoprodol and meprobamate in urine and plasma using liquid chromatography-tandem mass spectrometry (LC-MS/MS) / Matthew H. Slawson and Kamisha L. Johnson-Davis
  • Cetirizine quantification by high-performance liquid chromatography tandem mass spectrometry (LC-MS/MS) / Ada Munar [and others]
  • Quantification of docetaxel in serum using turbulent flow liquid chromatography electrospray tandem mass spectrometry (TFC-HPLC-ESI-MS/MS) / Christopher A. Crutchfield, Mark A. Marzinke, and William A. Clarke
  • Comprehensive urine drug screen by gas chromatography/mass spectrometry (GC/MS) / Bheemraj Ramoo [and others]
  • Broad-spectrum drug screening using liquid chromatography-hybrid triple-quadrupole linear ion trap mass spectrometry / Judy Stone
  • High-resolution mass spectrometry for untargeted drug screening / Alan H.B. Wu and Jennifer Colby
  • Quantitation of ethyl glucuronide and ethyl sulfate in urine using liquid chromatography-tandem mass spectrometry (LC-MS/MS) / Matthew H. Slawson and Kamisha L. Johnson-Davis
  • Quantification of hydroxychloroquine in blood using turbulent flow liquid chromatography-tandem mass spectrometry (TFLC-MS/MS) / Allison B. Chambliss, Anna K. Füzéry, and William A. Clarke
  • Quantification of iohexol in serum by high-performance liquid chromatography-tandem mass spectrometry (LC- MS/MS) / Faye B. Vicente [and others]
  • Quantitation of teriflunomide in human serum/plasma across a 40,000-fold concentration range by LC/MS/MS / Geoffrey S. Rule, Alan L. Rockwood, and Kamisha L. Johnson-Davis
  • Determination of menthol in plasma and urine by gas chromatography/mass spectrometry (GC/MS) / Judy Peat [and others]
  • Development of an assay for methotrexate and Its metabolites 7-hydroxy methotrexate and DAMPA in serum by LC-MS/MS / Ryan C. Schofield [and others]
  • Quantitative, multidrug pain medication testing by liquid chromatography : tandem mass spectrometry (LC-MS/MS) / Geza S. Bodor
  • Quantification of free phenytoin by liquid chromatography tandem mass spectrometry (LC/MS/MS) / Judy Peat, Clint Frazee, and Uttam Garg
  • Detection of stimulants and narcotics by liquid chromatography-tandem mass spectrometry and gas chromatography-mass spectrometry for sports doping control / Brian D. Ahrens, Yulia Kucherova, and Anthony W. Butch
  • Quantification of tricyclic antidepressants in serum using liquid chromatography electrospray tandem mass spectrometry (HPLC-ESI-MS/MS) / Christopher A. Crutchfield, Autumn R. Breaud, and William A. Clarke.
This volume describes methods and protocols for a number of drugs and toxins in a stepwise manner. Chapters in the book cover a wide array of topics such as: quantitation of Flecainide, Mexiletine, Propafenone, and Amiodarone in Serum or Plasma; quantitation of total Buprenorphine and Norbuprenorphine in Meconium; quantitation or Carisoprodol and Meprobamate in Urine; and quantitation of Tricyclic Antidepressants in Serum. Each chapter contains a brief introduction to the topic, clinical utility of the analyte(s), and useful notes to help laboratorians easily reproduce the protocols discussed. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and thorough, Clinical Applications of Mass Spectrometry in Drug Analysis: Methods and Protocols, is a great resource for laboratorians who are already using mass spectrometry or thinking of introducing this technology to their laboratories.
(source: Nielsen Book Data)9781493932511 20160619
Biology Library (Falconer)
Book
1 online resource (9 p. ) : digital, PDF file.
Terpenoids, naturally occurring compounds derived from isoprene units present in pine oleoresin, are a valuable source of chemicals used in solvents, fragrances, flavors, and have shown potential use as a biofuel. This paper describes a method to extract and analyze the terpenoids present in loblolly pine saplings and pine lighter wood. Various extraction solvents were tested over different times and temperatures. Samples were analyzed by pyrolysis-molecular beam mass spectrometry before and after extractions to monitor the extraction efficiency. The pyrolysis studies indicated that the optimal extraction method used a 1:1 hexane/acetone solvent system at 22°C for 1 h. Extracts from the hexane/acetone experiments were analyzed using a low thermal mass modular accelerated column heater for fast-GC/FID analysis. The most abundant terpenoids from the pine samples were quantified, using standard curves, and included the monoterpenes, α- and β-pinene, camphene, and δ-carene. Sesquiterpenes analyzed included caryophyllene, humulene, and α-bisabolene. In conclusion, diterpenoid resin acids were quantified in derivatized extractions, including pimaric, isopimaric, levopimaric, palustric, dehydroabietic, abietic, and neoabietic acids.
Book
xxiii, 350 pages, 46 unnumbered pages of plates : illustrations (some color) ; 25 cm
Hydrogen exchange mass spectrometry is widely recognized for its ability to probe the structure and dynamics of proteins. The application of this technique is becoming widespread due to its versatility for providing structural information about challenging biological macromolecules such as antibodies, flexible proteins and glycoproteins. Although the technique has been around for 25 years, this is the first definitive book devoted entirely to the topic. Hydrogen Exchange Mass Spectrometry of Proteins: Fundamentals, Methods and Applications brings into one comprehensive volume the theory, instrumentation and applications of Hydrogen Exchange Mass Spectrometry (HX-MS) - a technique relevant to bioanalytical chemistry, protein science and pharmaceuticals. The book provides a solid foundation in the basics of the technique and data interpretation to inform readers of current research in the method, and provides illustrative examples of its use in bio- and pharmaceutical chemistry and biophysics In-depth chapters on the fundamental theory of hydrogen exchange, and tutorial chapters on measurement and data analysis provide the essential background for those ready to adopt HX-MS. Expert users may advance their current understanding through chapters on methods including membrane protein analysis, alternative proteases, millisecond hydrogen exchange, top-down mass spectrometry, histidine exchange and method validation. All readers can explore the diversity of HX-MS applications in areas such as ligand binding, membrane proteins, drug discovery, therapeutic protein formulation, biocomparability, and intrinsically disordered proteins.
(source: Nielsen Book Data)9781118616499 20160704
Biology Library (Falconer)
Book
1 online resource (Article No. 026103 ) : digital, PDF file.
Empirical observations show that sodium(Na) is a benign contaminant in some thin-filmsolar cells. Here, we intentionally contaminate thermally evaporated tin sulfide (SnS)thin-films with sodium and measure the SnS absorber properties and solar cellcharacteristics. The carrier concentration increases from 2 × 10<sup>16</sup> cm<sup>-3</sup> to 4.3 × 10<sup>17</sup> cm<sup>-3</sup> in Na-doped SnSthin-films, when using a 13 nm NaCl seed layer, which is detrimental for SnS photovoltaic applications but could make Na-doped SnS an attractive candidate in thermoelectrics. We observed trends in carrier concentration and found that it is in good agreement with density functional theory calculations, which predict an acceptor-type NaSn defect with low formation energy.
Book
xii, 298 p. : ill. ; 25 cm
Introduction to Protein Mass Spectrometry provides a comprehensive overview of this increasingly important, yet complex, analytical technique. Unlike many other methods which automatically yield an absolutely unique protein name as output, protein mass spectrometry generally requires a deduction of protein identity from determination of peptide fragmentation products. This book enables readers to both understand, and appreciate, how determinations about protein identity from mass spectrometric data are made. Coverage begins with the technical basics, including preparations, instruments, and spectrometric analysis of peptides and proteins, before exploring applied use in biological applications, bioinformatics, database, and software resources. Citing the most recent and relevant work in the field of biological mass spectrometry, the book is written for researchers and scientists new to the field, but is also an ideal resource for those hoping to hone their analytical abilities. * Offers introductory information for scientists and researchers new to the field, as well as advanced insight into the critical assessment of computer-analyzed mass spectrometric results and their current limitations* Provides examples of commonly-used MS instruments from Bruker, Applied Biosystems, JEOL, Thermo Scientific/Thermo Fisher Scientific, IU, and Waters* Includes biological applications and exploration of analytical tools and databases for bioinformatics.
(source: Nielsen Book Data)9780128051238 20160619
Biology Library (Falconer)
Book
xxviii, 466 pages : illustrations ; 24 cm.
Covers the area of lipidomics from fundamentals and theory to applications * Presents a balanced discussion of the fundamentals, theory, experimental methods and applications of lipidomics * Covers different characterizations of lipids including Glycerophospholipids; Sphingolipids; Glycerolipids and Glycolipids; and Fatty Acids and Modified Fatty Acids * Includes a section on quantification of Lipids in Lipidomics such as sample preparation; factors affecting accurate quantification; and data processing and interpretation * Details applications of Lipidomics Tools including for Health and Disease; Plant Lipidomics; and Lipidomics on Cellular Membranes.
(source: Nielsen Book Data)9781118893128 20160704
Biology Library (Falconer)
Book
1 online resource ()
Mass Spectrometry: Techniques for the Structural Characterization of Glycans presents new methods for conducting detailed carbohydrate qualitative analysis-arming analytical chemists, pharmaceutical scientists, and food scientists with a quick reference that will allow them to determine the structures of carbohydrates molecules. As there is a need in the scientific community for content specific to structural determination and analysis of new glycoprotein drug, and because structure-activity analysis requires a structural determination of the N- and O-linked oligosaccharides linked to glycol-proteins, this book provides the relevant research that are necessary for advances and new outcomes in this area of study.
Book
1 online resource (18 p. ) : digital, PDF file.
The ARABIDOPSIS SKP1-LIKE1 (ASK1) protein functions as a subunit of SKP1-CUL1-F-box (SCF) E3 ubiquitin ligases. Previous genetic studies showed that ASK1 plays important roles in Arabidopsis flower development and male meiosis. However, the molecular impact of ASK1-containing SCF E3 ubiquitin ligases (ASK1-E3s) on the floral proteome and transcriptome is unknown. Here we identified proteins that are potentially regulated by ASK1-E3s by comparing floral bud proteomes of wild-type and the ask1 mutant plants. More than 200 proteins were detected in the ask1 mutant but not in wild-type and >300 were detected at higher levels in the ask1 mutant than in wild-type, but their RNA levels were not significantly different between wild-type and ask1 floral buds as shown by transcriptomics analysis, suggesting that they are likely regulated at the protein level by ASK1-E3s. Integrated analyses of floral proteomics and transcriptomics of ask1 and wild-type uncovered several potential aspects of ASK1-E3 functions, including regulation of transcription regulators, kinases, peptidases, and ribosomal proteins, with implications on possible mechanisms of ASK1-E3 functions in floral development. In conclusion, our results suggested that ASK1-E3s play important roles in Arabidopsis protein degradation during flower development. This study opens up new possibilities for further functional studies of these candidate E3 substrates.
Book
xiii, 306 pages : illustrations (some color) ; 26 cm.
  • Increased depth and breadth of plasma protein quantitation via two-dimensional liquid chromatography/multiple reaction monitoring-mass spectrometry with labeled peptide standards / Andrew J. Percy ... [et al.]
  • Quantitative analysis of the Sirt5-regulated lysine succinylation proteome in mammalian cells / Yue Chen
  • Determining the composition and stability of protein complexes using an integrated label-free and stable isotope labeling strategy / Todd M. Greco, Amanda J. Guise, and Ileana M. Cristea
  • Label-free quantitation for clinical proteomics / Robert Moulder, Young Ah Goo, and David R. Goodlett
  • Proteogenomic methods to improve genome annotation / Keshava K. Datta, Anil K. Madugundu, and Harsha Gowda
  • Mass spectrometry-based quantitative O-GlcNAcomic analysis / Junfeng Ma and Gerald W. Hart
  • Isolating and quantifying plasma HDL proteins by sequential density gradient ultracentrifugation and targeted proteomics / Clark M. Henderson, Tomas Vaisar, and Andrew N. Hoofnagle
  • Method for label-free, differential top-down proteomics / Ioanna Ntai ... [et al.]
  • Multiplexed immunoaffinity enrichment of peptides with anti-peptide antibodies and quantification by stable isotope dilution multiple reaction monitoring mass spectrometry / Eric Kuhn and Steven A. Carr
  • High-throughput quantitative proteomics enabled by mass defect-based 12-plex DiLeu isobaric tags / Dustin C. Frost and Lingjun Li
  • Isotopic N, N-Dimethyl leucine (iDiLeu) for absolute quantification of peptides using a standard curve approach / Tyler Greer and Lingjun Li
  • Selecting optimal peptides for targeted proteomic experiments in human plasma using in vitro synthesized proteins as analytical standards / James G. Bollinger ... [et al.]
  • Using the CPTAC assay portal to identify and implement highly characterized targeted proteomics assays / Jeffrey R. Whiteaker ... [et al.]
  • Large-scale and deep quantitative proteome profiling using isobaric labeling coupled with two-dimensional LC-MS/MS / Marina A. Gritsenko ... [et al.]
  • Multiple and selective reaction monitoring using triple quadrupole mass spectrometer : preclinical large cohort analysis / Qin Fu ... [et al.]
  • Methods for SWATH™ : data independent acquisition on tripleTOF mass spectrometers / Ronald J. Holewinski ... [et al.]
  • Measurement of phosphorylated peptides with absolute quantification / Raven J. Reddy ... [et al.]
  • Proteomic analysis of protein turnover by metabolic whole rodent pulse-chase isotopic labeling and shotgun mass spectrometry analysis / Jeffrey N. Savas, Sung Kyu Park, and John R. Yates, III.
This volume describes prominent methodologies developed by laboratories that have been leading the field of quantitative proteomics by mass spectrometry. The procedures for performing the experiments are described in an easy-to-understand manner with many technical details that usually are not reported in typical research articles. This second edition of Quantitative Proteomics by Mass Spectrometry provides a broad perspective of the methodologies used for quantifying proteins and post-translational modifications in different types of biomedical specimens. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and thorough, Quantitative Proteomics by Mass Spectrometry, Second Edition is a valuable resource to help researchers understand and learn about the latest tools used in the study of quantitative proteomics by mass spectrometry.
(source: Nielsen Book Data)9781493935222 20160704
Biology Library (Falconer)
Book
1 online resource (xviii, 176 pages) : illustrations (some color).
Book
1 online resource.
  • An Introduction to Ambient Ionization Mass Spectrometry-- Direct Analysis in real time (DART(R))-- Ionization Mechanisms of Direct Analysis in Real Time (DART)-- Atmospheric Samples Analysis Probe (ASAP) Mass Spectrometry-- Ambient Analysis by Thermal Desorption Atmospheric Pressure Photoionization-- Low Temperature Plasma Probe-- Flowing Atmospheric Pressure Afterglow (FAPA), the Plasma-based Source for your ADI-MS needs-- Spray Desorption Collection and DESI Mechanisms-- Easy Ambient Sonic-Spray Ionization-- Secondary Electrospray Ionization-- Probe Electrospray Ionization-- Desorption Electrospray Mass Spectrometry-- Surface Acoustic Wave Nebulization-- Laser Ablation Electrospray Ionization Mass Spectrometry: Mechanisms, Configurations and Imaging Applications-- Electrospray Laser Desorption Ionization Mass Spectrometry-- Paper Spray-- Inlet and Vacuum Ionization from Ambient Conditions-- Enabling Automated Sample Analysis by Direct Analysis in Real Time (DART) Mass Spectrometry-- Laser Ablation Electrospray Ionization Mass Spectrometry (LAESI(R)-MS): Ambient Ionization Technology for 2D and 3D Molecular Imaging-- Liquid Extraction Surface Analysis Mass Spectrometry (LESA MS): Combining Liquid Extraction, Surface Profiling and Ambient Ionization Mass Spectrometry in One Novel Analysis Technique-- Subject Index.
  • (source: Nielsen Book Data)9781849739269 20160618
Ambient ionization has emerged as one of the hottest and fastest growing topics in mass spectrometry enabling sample analysis with minimal sample preparation. Introducing the subject and explaining the basic concepts and terminology, this book will provide a comprehensive, unique treatise devoted to the subject. Written by acknowledged experts, there are full descriptions on how new ionization techniques work, with an overview of their strengths, weaknesses and applications. This title will bring the reader right up to date, with both applications and theory, and will be suitable as a tutorial text for those starting in the field from a variety of disciplines.
(source: Nielsen Book Data)9781849739269 20160618
Book
xxii, 378 pages : illustrations (some color) ; 25 cm
  • List of Contributors XIII Preface XVII Abbreviations XIX 1 Introduction to Mass Spectrometry, a Tutorial 1 Wilfried M.A. Niessen and David Falck 1.1 Introduction 1 1.2 Figures of Merit 1 1.2.1 Introduction 1 1.2.2 Resolution 2 1.2.3 Mass Accuracy 4 1.2.4 General Data Acquisition in MS 5 1.3 Analyte Ionization 6 1.3.1 Introduction 6 1.3.2 Electrospray Ionization 8 1.3.3 Matrix-Assisted Laser Desorption Ionization 10 1.3.4 Other Ionization Methods 10 1.3.5 Solvent and Sample Compatibility Issues 11 1.4 Mass Analyzer Building Blocks 12 1.4.1 Introduction 12 1.4.2 Quadrupole Mass Analyzer 13 1.4.3 Ion-Trap Mass Analyzer 13 1.4.4 Time-of-Flight Mass Analyzer 15 1.4.5 Fourier Transform Ion Cyclotron Resonance Mass Spectrometer 16 1.4.6 Orbitrap Mass Analyzer 17 1.4.7 Ion Detection 18 1.5 Tandem Mass Spectrometry 18 1.5.1 Introduction: Tandem-in-Time and Tandem-in-Space 18 1.5.2 Ion Dissociation Techniques 20 1.5.3 Tandem Quadrupole MS MS Instruments 21 1.5.4 Ion-Trap MSn Instruments 23 1.5.5 Tandem TOF (TOF TOF) Instruments 23 1.5.6 Hybrid Instruments (Q TOF, Q LIT, IT TOF) 24 1.5.7 MS MS and MSn in FT-ICR-MS 26 1.5.8 Orbitrap-Based Hybrid Systems 27 1.5.9 Ion-Mobility Spectrometry Mass Spectrometry 28 1.6 Data Interpretation and Analytical Strategies 30 1.6.1 Data Acquisition in MS Revisited 30 1.6.2 Quantitative Bioanalysis and Residue Analysis 31 1.6.3 Identification of Small-Molecule Known Unknowns 32 1.6.4 Identification of Drug Metabolites 33 1.6.5 Protein Molecular Weight Determination 37 1.6.6 Peptide Fragmentation and Sequencing 38 1.6.7 General Proteomics Strategies: Top-Down, Middle-Down, Bottom-Up 39 1.7 Conclusion and Perspectives 43 References 43 Part I Direct MS Based Affinity Techniques 55 2 Studying Protein Protein Interactions by Combining Native Mass Spectrometry and Chemical Cross-Linking 57 Michal Sharon and Andrea Sinz 2.1 Introduction 57 2.2 Protein Analysis by Mass Spectrometry 58 2.3 Native MS 59 2.3.1 Instrumentation for High-mass ion Detection 60 2.3.2 Defining the Exact Mass of the Composing Subunits 60 2.3.3 Analyzing the Intact Complex 61 2.4 Chemical Cross-linking MS 64 2.4.1 Types of Cross-linkers 64 2.4.2 MS/MS Cleavable Cross-linkers 66 2.4.3 Data Analysis 68 2.5 Value of Combining NativeMS with Chemical Cross-linkingMS 68 2.6 Regulating the Giant 69 2.7 Capturing Transient Interactions 70 2.8 An Integrative Approach for Obtaining Low-Resolution Structures of Native Protein Complexes 72 2.9 Future Directions 73 References 74 3 Native Mass Spectrometry Approaches Using Ion Mobility-Mass Spectrometry 81 Frederik Lermyte, Esther Marie Martin, Albert Konijnenberg, Filip Lemiere, and Frank Sobott 3.1 Introduction 81 3.2 Sample Preparation 82 3.3 Electrospray Ionization 84 3.4 Mass Analyzers and Tandem MS Approaches 88 3.5 Ion Mobility 90 3.6 Data Processing 95 3.7 Challenges and Future Perspectives 98 References 102 Part II LC MS Based with Indirect Assays 109 4 Methodologies for Effect-Directed Analysis: Environmental Applications, Food Analysis, and Drug Discovery 111 Willem Jonker, Marja Lamoree, Corine J. Houtman, and Jeroen Kool 4.1 Introduction 111 4.2 Principle of Traditional Effect-Directed Analysis 113 4.3 Sample Preparation 113 4.3.1 Environmental Analysis 113 4.3.2 Food Analysis 121 4.3.3 Drug Discovery 124 4.4 Fractionation for Bioassay Testing 126 4.4.1 Environmental Analysis 126 4.4.2 Food Analysis 130 4.4.3 Drug Discovery 131 4.5 Miscellaneous Approaches 133 4.6 Bioassay Testing 136 4.6.1 Environmental Analysis 136 4.6.2 Food Analysis 140 4.6.3 Drug Discovery 140 4.7 Identification and Confirmation Process 141 4.7.1 Instrumentation 141 4.7.2 Data Analysis 143 4.8 Conclusion and Perspectives 148 References 149 5 MS Binding Assays 165 Georg Hofner and Klaus T.Wanner 5.1 Introduction 165 5.2 MS Binding Assays Strategy 167 5.2.1 Analogies and Differences Compared to Radioligand Binding Assays 167 5.2.2 Fundamental Assay Considerations 169 5.2.3 Fundamental Analytical Considerations 170 5.3 Application of MS Binding Assays 171 5.3.1 MS Binding Assays for the GABA Transporter GAT1 171 5.3.2 MS Binding Assays for the Serotonin Transporter 183 5.3.3 MS Binding Assays Based on the Quantitation of the Nonbound Marker 187 5.3.4 Other Examples Following the Concept of MS Binding Assays 189 5.4 Summary and Perspectives 191 Acknowledgments 192 References 192 6 Metabolic Profiling Approaches for the Identification of Bioactive Metabolites in Plants 199 Emily Pipan and Angela I. Calderon 6.1 Introduction to Plant Metabolic Profiling 199 6.2 Sample Collection and Processing 200 6.3 Hyphenated Techniques 203 6.3.1 Liquid Chromatography Mass Spectrometry 203 6.3.2 Gas Chromatography Mass Spectrometry 206 6.3.3 Capillary Electrophoresis Mass Spectrometry 207 6.4 Mass Spectrometry 207 6.4.1 Time of Flight 208 6.4.2 Quadrupole Mass Filter 208 6.4.3 Ion Traps (Orbitrap and Linear Quadrupole (LTQ)) 209 6.4.4 Fourier Transform Mass Spectrometry 210 6.4.5 Ion Mobility Mass Spectrometry 210 6.5 Mass Spectrometric Imaging 210 6.5.1 MALDI-MS 211 6.5.2 SIMS-MS 212 6.5.3 DESI-MS 212 6.5.4 LAESI-MS 213 6.5.5 LDI-MS and Others for Imaging 213 6.6 Data Analysis 214 6.6.1 Data Processing 214 6.6.2 Data Analysis Methods 214 6.6.3 Databases 215 6.7 Future Perspectives 216 References 216 7 Antivenomics: A Proteomics Tool for Studying the Immunoreactivity of Antivenoms 227 Juan J. Calvete, Jose Maria Gutierrez, Libia Sanz, Davinia Pla, and Bruno Lomonte 7.1 Introduction 227 7.2 Challenge of Fighting Human Envenoming by Snakebites 227 7.3 Toolbox for Studying the Immunological Profile of Antivenoms 228 7.4 First-Generation Antivenomics 229 7.5 Snake Venomics 230 7.6 Second-Generation Antivenomics 232 7.7 Concluding Remarks 236 Acknowledgments 236 References 236 Part III Direct Pre- and On-Column Coupled Techniques 241 8 Frontal and Zonal Affinity Chromatography Coupled to Mass Spectrometry 243 Nagendra S. Singh, Zhenjing Jiang, and Ruin Moaddel 8.1 Introduction 243 8.2 Frontal Affinity Chromatography 244 8.3 Staircase Method 247 8.4 Simultaneous Frontal Analysis of a Complex Mixture 249 8.5 Multiprotein Stationary Phase 252 8.6 Zonal Chromatography 253 8.7 Nonlinear Chromatography 260 Acknowledgments 265 References 265 9 Online Affinity Assessment and Immunoaffinity Sample Pretreatment in Capillary Electrophoresis Mass Spectrometry 271 Rob Haselberg and Govert W. Somsen 9.1 Introduction 271 9.2 Capillary Electrophoresis 272 9.3 Affinity Capillary Electrophoresis 276 9.3.1 Dynamic Equilibrium ACE (Fast Complexation Kinetics) 276 9.3.2 Pre-Equilibrium ACE (Slow Complexation Kinetics) 279 9.3.3 Kinetic ACE (Intermediate Complexation Kinetics) 280 9.4 Immunoaffinity Capillary Electrophoresis 281 9.5 Capillary Electrophoresis Mass Spectrometry 283 9.5.1 General Requirements for Effective CE MS Coupling 283 9.5.2 Specific Requirements for ACE MS and IA-CE-MS 284 9.6 Application of ACE MS 286 9.7 Applications of IA-CE MS 292 9.8 Conclusions 295 References 296 10 Label-Free Biosensor Affinity Analysis Coupled to Mass Spectrometry 299 David Bonnel, Dora Mehn, and Gerardo R. Marchesini 10.1 Introduction to MS-Coupled Biosensor Platforms 299 10.2 Strategies for Coupling Label-Free Analysis with Mass Spectrometry 301 10.2.1 On-Chip Approaches 301 10.2.2 Off-Chip Configurations 305 10.2.3 Chip Capture and Release Chromatography Electrospray-MS 306 10.3 New Sensor and MS Platforms, Opportunities for Integration 307 10.3.1 Imaging Nanoplasmonics 307 10.3.2 EvanescentWave SiliconWaveguides 308 10.3.3 New Trends in MS Matrix-Free Ion Sources 309 10.3.4 Tag-Mass 310 10.3.5 Integration 310 References 310 Part IV Direct Post Column Coupled Affinity Techniques 317 11 High-Resolution Screening: Post-Column Continuous-Flow Bioassays 319 David Falck, Wilfried M.A. Niessen, and Jeroen Kool 11.1 Introduction 319 11.1.1 Variants of On-line Post-Column Assays Using Mass Spectrometry 321 11.1.2 Targets and Analytes 328 11.2 The High-Resolution Screening Platform 330 11.2.1 Separation 330 11.2.2 Flow Splitting 334 11.2.3 Bioassay 336 11.2.4 MS Detection 340 11.3 Data Analysis 342 11.3.1 Differences between HRS and HTS 342 11.3.2 Validation 350 11.4 Conclusions and Perspectives 353 11.4.1 The Relation of On-line Post-Column Assays to Other Formats 353 11.4.2 Trends in High-Resolution Screening 354 11.4.3 Conclusions 357 References 358 12 Conclusions 365 Jeroen Kool Index 373.
  • (source: Nielsen Book Data)9783527334643 20160618
This monograph reviews all relevant technologies based on mass spectrometry that are used to study or screen biological interactions in general. Arranged in three parts, the text begins by reviewing techniques nowadays almost considered classical, such as affinity chromatography and ultrafiltration, as well as the latest techniques. The second part focusses on all MS-based methods for the study of interactions of proteins with all classes of biomolecules. Besides pull down-based approaches, this section also emphasizes the use of ion mobility MS, capture-compound approaches, chemical proteomics and interactomics. The third and final part discusses other important technologies frequently employed in interaction studies, such as biosensors and microarrays. For pharmaceutical, analytical, protein, environmental and biochemists, as well as those working in pharmaceutical and analytical laboratories.
(source: Nielsen Book Data)9783527334643 20160618
Biology Library (Falconer)
Book
1 online resource.
  • Front Cover; Anthropic Awareness: The Human Aspects of Scientific Thinking in NMR Spectroscopy and Mass Spectrometry; Copyright; Contents; Contributors; Preface; Editor's Personal Acknowledgments; Part I: ``Anthropic Awareness (AA) ́́(Mind your mind!); Chapter 1: The Philosophy of ``Anthropic Awareness ́́in Scientific Thinking; 1.1. Introduction; 1.2. The Pillars; Pillar 1. AA Is a Tool; Pillar 2. The Definition of ``Science; ́́ Pillar 3. The Concepts of ``Science ́́and ``Scientific Truth; ́́ Pillar 4. The AA Model of Scientific Thinking
  • Pillar 5. On the Meaning of ``Description ́́and ``UnderstandingṔ́illar 6. The Triangle of Understanding; Pillar 7. The Relationship Between the AA Model of Thinking and the Triangle of Understanding; Pillar 8. Language; Pillar 9. The Definition of Definition; Pillar 10. Scientific Hypotheses, Models, Theories, Laws, Explanations, Metaphors, and Metaphoric Models; Pillar 11. Creativity in Science; Pillar 12. Scientific Communication; Pillar 13. Sound and Unsound Models; Pillar 14. The Role of Refutation in Science; Pillar 15. The Practical Versus Theoretical Significance of Exposing Delusors
  • Pillar 16. Paradigm NestsPillar 17. ``Forward ́́and ``Backward ́́Scientific Research; Pillar 18. The Meaning of ``New ́́Scientific Result; Pillar 19. The Meaning of ``Significant ́́Scientific Result; Pillar 20. Reporting Scientific Results; Pillar 21. The ``Spideric ́́Nature of a Scientific Problem; Pillar 22. AA in the Context of the Literature and Other Initiatives Addressing Cognitive Errors; Pillar 23. ``Everyday Thinking ́́Versus ``Scientific Thinking; ́́ Pillar 24. The Trap-Experience; Pillar 25. The Dual Nature of Mental Traps
  • Pillar 26. Mental Traps in Relation to Scientific Knowledge and Intellect (``Educated Error)́́Pillar 27. The Relationship and Synergy of Mental Traps; Pillar 28. Identifying the Mental Traps; Pillar 29. Trap-Blindness and Avoiding Mental Traps; Pillar 30. Trap-Consciousness and the ``Sacredness ́́of Science; 1.3. Mental Traps (Mind Your Mind!); Interlude; Mental Trap (Master Trap) #1. We Seek Mental Security (the ``Enjoy-Your-Flight ́́Effect); Mental Trap (Master Trap) #2. We Have An Instinctive Urge to Interpret Data; Mental Trap (Master Trap) #3. Belief Dominates Over Reason
  • Mental Trap #4. The Initial Belief SyndromeMental Trap #5. We Accept Anecdotal Evidence; Mental Trap #6. We Tend to Trust Authority Without Question (Might is Right); Mental Trap #7. We Go With the Crowd (Herd Instinct); Mental Trap #8. We Accept Knowledge Based on Tradition; Mental Trap #9. We Think Inside Our Paradigm Nests; Mental Trap #10. We Accept Intuitively Appealing Explanations; Mental Trap #11. We Confuse Mathematical Descriptions with a Physical Understanding; Mental Trap #12. We Project the Absolute Truths of Mathematics onto Physics
Anthropic Awareness: The Human Aspects of Scientific Thinking in NMR Spectroscopy and Mass Spectrometry blends psychology, philosophy, physics, mathematics, and chemistry, describing a human-centered philosophy of the essence of scientific thinking in the natural sciences and in everyday life. It addresses the reasons why we are prone to make errors in our conclusions and how to avoid such mistakes, also exploring a number of the "mental traps" that can lead to both individual mistakes and mass misconceptions. The book advocates that by understanding the nature of these mental traps we can adopt tactics to safely evade them. It includes Illustrative examples of common scientific misunderstandings and mental traps in both the theory and real-life application of NMR spectroscopy and mass spectrometry.

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