Coorperative folding kinetics of BBL protein and peripheral subunit-binding domain homologues
- Authors
- Wookyung Yu; Kwanghoon Chung; Mookyung Cheon; Muyoung Heo; Kyou-hoon Han; Sihyun Ham; Iksoo Chang
- Issue Date
- Feb-2008
- Publisher
- NATL ACAD SCIENCES
- Citation
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.105, no. 7, pp 2397 - 2402
- Journal Title
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Volume
- 105
- Number
- 7
- Start Page
- 2397
- End Page
- 2402
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/14344
- DOI
- 10.1073/pnas.0708480105
- ISSN
- 0027-8424
1091-6490
- Abstract
- Recent experiments claiming that Naf-BBL protein follows a global downhill folding raised an important controversy as to the folding mechanism of fast-folding proteins. Under the global downhill folding scenario, not only do proteins undergo a gradual folding, but folding events along the continuous folding pathway also could be mapped out from the equilibrium denaturation experiment. Based on the exact calculation using a free energy landscape, relaxation eigenmodes from a master equation, and Monte Carlo simulation of an extended Muñoz–Eaton model that incorporates multiscale-heterogeneous pairwise interactions between amino acids, here we show that the very nature of a two-state cooperative transition such as a bimodal distribution from an exact free energy landscape and biphasic relaxation kinetics manifest in the thermodynamics and folding–unfolding kinetics of BBL and peripheral subunit-binding domain homologues. Our results provide an unequivocal resolution to the fundamental controversy related to the global downhill folding scheme, whose applicability to other proteins should be critically reexamined.
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