Understanding protein folding via free-energy surfaces from theory and experiment

Citation
Ar. Dinner et al., Understanding protein folding via free-energy surfaces from theory and experiment, TRENDS BIOC, 25(7), 2000, pp. 331-339
Citations number
68
Categorie Soggetti
Biochemistry & Biophysics
Journal title
TRENDS IN BIOCHEMICAL SCIENCES
ISSN journal
09680004 → ACNP
Volume
25
Issue
7
Year of publication
2000
Pages
331 - 339
Database
ISI
SICI code
0968-0004(200007)25:7<331:UPFVFS>2.0.ZU;2-8
Abstract
The ability of protein molecules to fold into their highly structured funct ional states is one of the most remarkable evolutionary achievements of bio logy. In recent years, our understanding of the way in which this complex s elf-assembly process takes place has increased dramatically. Much of the re ason for this advance has been the development of energy surfaces (landscap es), which allow the folding reaction to be described and visualized in a m eaningful manner. Analysis of these surfaces, derived from the constructive interplay between theory and experiment, has led to the development of a u nified mechanism for folding and a recognition of the underlying factors th at control the rates and products of the folding process.