Work

Identifying the protein folding nucleus using molecular dynamics

Year: 2000

Type: article

Abstract: Molecular dynamics simulations of folding in an off-lattice protein model reveal a nucleation scenario, in which a few well-defined contacts are formed with high probability in the transition state ensemble of conformations. Their appearance determines folding cooperativity and drives the model protein into its folded conformation. Amino acid residues participating in those contacts may serve as "accelerator pedals" used by molecular evolution to control protein folding rate.

Source: Journal of Molecular Biology

DOI: 10.1006/jmbi.1999.3534

Authors: Nikolay V. Dokholyan, Sergey V. Buldyrev, H.Eugene Stanley, Eugene I. Shakhnovich

Institutions: Boston University, Harvard University

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,730

Funders: National Science Foundation, National Institutes of Health, U.S. Public Health Service, National Institute of General Medical Sciences