Quantifying side-chain conformational variations in protein structure
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep37024.pdf
Reference36 articles.
1. Marcos, M. L. & Echave, J. Too packed to change: side-chain packing and site-specific substitution rates in protein evolution. PeerJ 3, e911, doi: 10.7717/peerj.911 (2015).
2. Bernhard, S. A. & MacQuarrie, R. A. Half-site reactivity and the “induced-fit” hypothesis. Journal of molecular biology 74, 73–78 (1973).
3. Larriva, M. & Rey, A. Design of a rotamer library for coarse-grained models in protein-folding simulations. Journal of chemical information and modeling 54, 302–313, doi: 10.1021/ci4005833 (2014).
4. Wang, C., Schueler-Furman, O. & Baker, D. Improved side-chain modeling for protein-protein docking. Protein Sci 14, 1328–1339, doi: 10.1110/ps.041222905 (2005).
5. Ollikainen, N., de Jong, R. M. & Kortemme, T. Coupling Protein Side-Chain and Backbone Flexibility Improves the Re-design of Protein-Ligand Specificity. PLoS computational biology 11, e1004335, doi: 10.1371/journal.pcbi.1004335 (2015).
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