Surveying biomolecular frustration at atomic resolution.

ABSTRACT: To function, biomolecules require sufficient specificity of interaction as well as stability to live in the cell while still being able to move. Thermodynamic stability of only a limited number of specific structures is important so as to prevent promiscuous interactions. The individual interactions in proteins, therefore, have evolved collectively to give funneled minimally frustrated landscapes but some strategic parts of biomolecular sequences located at specific sites in the structure have been selected to be frustrated in order to allow both motion and interaction with partners. We describe a framework efficiently to quantify and localize biomolecular frustration at atomic resolution by examining the statistics of the energy changes that occur when the local environment of a site is c

SUBMITTER: Chen M 

PROVIDER: S-EPMC7683549 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature