Nicholas J. Lyle, Ph.D.
Affiliations: | 2013 | Biology & Biomedical Sciences (Computational & Systems Biology) | Washington University, Saint Louis, St. Louis, MO |
Area:
General BiophysicsGoogle:
"Nicholas Lyle"Parents
Sign in to add mentor| Rohit V. Pappu | grad student | 2013 | Washington University | |
| (Quantification of conformational heterogeneity and its role in protein aggregation and unfolding.) | ||||
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Publications
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| Diamond MI, Cai S, Boudreau A, et al. (2015) Subcellular localization and Ser-137 phosphorylation regulate tumor-suppressive activity of profilin-1. The Journal of Biological Chemistry. 290: 9075-86 |
| Holehouse AS, Garai K, Lyle N, et al. (2015) Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation. Journal of the American Chemical Society. 137: 2984-95 |
| Mittal A, Lyle N, Harmon TS, et al. (2014) Hamiltonian Switch Metropolis Monte Carlo Simulations for Improved Conformational Sampling of Intrinsically Disordered Regions Tethered to Ordered Domains of Proteins. Journal of Chemical Theory and Computation. 10: 3550-3562 |
| Luan B, Lyle N, Pappu RV, et al. (2014) Denatured state ensembles with the same radii of gyration can form significantly different long-range contacts. Biochemistry. 53: 39-47 |
| Holehouse AS, Lyle N, Vitalis A, et al. (2014) Parsing the Contributions of Polypeptide Backbones and Sidechains to Denaturation in Concentrated Aqueous Solutions of Urea and Guanidinium Chloride Biophysical Journal. 106: 484a |
| Lyle N, Das RK, Pappu RV. (2013) A quantitative measure for protein conformational heterogeneity. The Journal of Chemical Physics. 139: 121907 |
| Meng W, Luan B, Lyle N, et al. (2013) The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9. Biochemistry. 52: 2662-71 |
| Meng W, Lyle N, Luan B, et al. (2013) Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure. Proceedings of the National Academy of Sciences of the United States of America. 110: 2123-8 |
| Mao AH, Lyle N, Pappu RV. (2013) Describing sequence-ensemble relationships for intrinsically disordered proteins. The Biochemical Journal. 449: 307-18 |
| Lyle NJ, Pappu RV. (2013) Quantifying Disorder using Simulated Ensembles for Different Classes of Polypeptides Biophysical Journal. 104: 53a |