Work

The capillarity picture and the kinetics of one-dimensional protein folding

Year: 2008

Type: article

Abstract: Energy landscape theory unites the study of protein folding with the theory of phase transitions. Dimensionality, whose key role in phase transitions is well known, comes to the fore in folding repeat proteins. Repeat proteins are made of near repetitions of 20–40 residues encoding recurring structural motifs. Each repeating element interacts only with its immediate neighbors, forming extended, globally one-dimensional structures that can be interrupted by thermally excited defects (1). The equilibrium properties of repeat proteins may be mapped onto a one-dimensional Ising model (2–4). Going beyond equilibrium, in this issue of PNAS, Werbeck et al. (5) delight us by studying the folding kinetics of a very long repeat protein, D34, a 12-ankyrin repeat fragment of AnkyrinR.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.0805287105

Authors: Diego U. Ferreiro, Peter G. Wolynes

Institution: University of California San Diego

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences

Award: IkB/NF-kB Recognition in Silico, In Vitro and In Vivo