Restricted sidechain plasticity in the structures of native proteins and complexes

TitleRestricted sidechain plasticity in the structures of native proteins and complexes
Publication TypeJournal Article
Year of Publication2011
AuthorsFleishman, S. J., Khare S. D., Koga N., & Baker D.
JournalProtein science
Volume20
Issue4
Pagination753-7
Date Published2011 Apr
ISSN1469-896X
KeywordsPrimary Publication
Abstract

Protein-design methodology can now generate models of protein structures and interfaces with computed energies in the range of those of naturally occurring structures. Comparison of the properties of native structures and complexes to isoenergetic design models can provide insight into the properties of the former that reflect selection pressure for factors beyond the energy of the native state. We report here that sidechains in native structures and interfaces are significantly more constrained than designed interfaces and structures with equal computed binding energy or stability, which may reflect selection against potentially deleterious non-native interactions.

DOI10.1002/pro.604
Alternate JournalProtein Sci.
AttachmentSize
fleishman11A.pdf295.85 KB