title: Restricted sidechain plasticity in the structures of native proteins and complexes.
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.
authors: Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
authors: Sarel J
authors: SJ
authors: Fleishman
authors: Sagar D
authors: SD
authors: Khare
authors: Nobuyasu
authors: N
authors: Koga
authors: David
authors: D
authors: Baker
mesh_terms: D003198:Computer Simulation; D030562:Databases, Protein; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D013816:Thermodynamics
chemical_list: D011506:Proteins