Work

Restricted sidechain plasticity in the structures of native proteins and complexes

Year: 2011

Type: article

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.

Source: Protein Science

DOI: 10.1002/pro.604

Authors: Sarel J. Fleishman, Sagar D. Khare, Nobuyasu Koga, David Baker

Institutions: University of Washington, Howard Hughes Medical Institute

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: Howard Hughes Medical Institute, Defense Threat Reduction Agency, Advanced Research Projects Agency, Japan Society for the Promotion of Science

OpenAlex ID: W1681479328

FWCI: 2.465

Cites: 24

Cited by: 55

Related to: 10