David A Snyder
Professor • Department of
My research lies at the intersection of computational and experimental biochemistry. In particular, I am interested in developing -- and exploring the mathematics underlying -- processing techniques (e.g. covariance NMR) that facilitate the use of NMR to explore the chemistry of complex mixtures. I am also interested in the evolution of protein flexibility and of "moonlighting" proteins as well as in the use of computational and spectroscopic techniques to identify protein ligands, in particular allosteric inhibitors of protein/small molecule and protein/protein interactions.
My Google Scholar page is https://scholar.google.com/citations?user=_Y2QjMgAAAAJ&hl=en&oi=sra and my ORCID page is https://orcid.org/0000-0001-6608-2975
I do most of my programming nowadays in MATLAB. My MATLAB central file exchange page is https://www.mathworks.com/matlabcentral/profile/authors/1420896 .
Computational Biochemistry, Nuclear Magnetic Resonance
Patterns in Protein Flexibility: A Comparison of NMR “Ensembles”, MD Trajectories, and Crystallographic B-Factors; Molecules; Volume
Protein Structure Prediction Assisted with Sparse NMR Data in CASP13; Proteins: Structure, Function and Genetics; Volume
Prediction of protein flexibility using a conformationally restrained contact map; , Proteins: Structure, Function and Bioinformatics; Volume
Analysis of ligand–protein exchange by Clustering of Ligand Diffusion Coefficient Pairs (CoLD-CoP); Journal of Magnetic Resonance; Volume
The expanded FindCore method for identification of a core atom set for assessment of protein structure prediction; , Proteins: Structure, Function, and Bioinformatics; Volume
Docking studies on tyrosinase and SARS-CoV2 nsp16: Discovery of novel enzymatic activities and drug repurposing
Current Perspectives in Covariance NMR
Notable Courses Taught
Biochemistry I (CHEM 4270)
Biochemistry II (CHEM 4280)
Chemistry for Health Sciences (CHEM 1330)
Theoretical and Physical Methods (CHEM 6004): Co-taught with Prof. J. Foley.