Repeat-protein folding: new insights into origins of cooperativity, stability, and topology.

ABSTRACT: Although our understanding of globular protein folding continues to advance, the irregular tertiary structures and high cooperativity of globular proteins complicates energetic dissection. Recently, proteins with regular, repetitive tertiary structures have been identified that sidestep limitations imposed by globular protein architecture. Here we review recent studies of repeat-protein folding. These studies uniquely advance our understanding of both the energetics and kinetics of protein folding. Equilibrium studies provide detailed maps of local stabilities, access to energy landscapes, insights into cooperativity, determination of nearest-neighbor interaction parameters using statistical thermodynamics, relationships between consensus sequences and repeat-protein stability. Kinetic stu

SUBMITTER: Kloss E 

PROVIDER: S-EPMC2474553 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature