Toward a quantitative theory of intrinsically disordered proteins and their function.

ABSTRACT: A large number of proteins are sufficiently unstable that their full 3D structure cannot be resolved. The origins of this intrinsic disorder are not well understood, but its ubiquitous presence undercuts the principle that a protein's structure determines its function. Here we present a quantitative theory that makes predictions regarding the role of intrinsic disorder in protein structure and function. In particular, we discuss the implications of analytical solutions of a series of fundamental thermodynamic models of protein interactions in which disordered proteins are characterized by positive folding free energies. We validate our predictions by assigning protein function by using the gene ontology classification--in which "protein binding", "catalytic activity", and "transcription re

SUBMITTER: Liu J 

PROVIDER: S-EPMC2775701 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature