Relating Protein Structure and Scalar Couplings: Improving the Karplus Relation
- Type of resource
- Date created
- June 14, 2015
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Honors theses written by undergraduates in the Stanford University Department of Biology, 2014-2015., Honors theses written by undergraduates in the Stanford University Department of Biology, 2014-2015.
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Intrinsically disordered proteins (IDPs) are implicated in an increasing number of neurodegenerative diseases, including Parkinson's, Alzheimer's, and Huntington's disease. While our knowledge of protein structures in the crystalline phase is advanced, IDPs do not readily crystallize, and the tools we have to study protein structure in solution are more limited. In this project, we integrated X-ray crystal-structure data from the PDB repository, solution-phase NMR spectroscopy data from the BMRB database, and molecular dynamics simulations to improve the accuracy of the Karplus Relation, an especially important but dated tool used towards solving the structures of solution-phase proteins. Improvement of the Karplus Relation would advance our understanding of protein dynamics and aid in small-molecule drug design.
- Preferred Citation
- El-Gabalawy, Osama M. and Pande, Vijay S. and Mudgett, Mary Beth. (2015). Relating Protein Structure and Scalar Couplings: Improving the Karplus Relation. Stanford Digital Repository. Available at: http://purl.stanford.edu/tk526dx0882
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