期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 99, 期 12, 页码 8019-8024出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.072220699
关键词
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资金
- NINDS NIH HHS [1R01 NS 41356-01, R01 NS041356] Funding Source: Medline
We report the thermodynamics and kinetics of an off-lattice Go model P-hairpin from Ig-binding protein confined to an inert spherical pore. Confinement enhances the stability of the hairpin due to the decrease in the entropy of the unfolded state. Compared with their values in the bulk, the rates of hairpin formation increase in the spherical pore. Surprisingly, the dependence of the rates on the pore radius, R-s, is nonmonotonic. The rates reach a maximum at R-s/R(g,N)(b)similar or equal to1.5, where R-g,N(b) is the radius of gyration of the folded beta-hairpin in the bulk. The denatured state ensemble of the encapsulated beta-hairpin is highly structured even at substantially elevated temperatures. Remarkably, a profound effect of confinement is evident even when the beta-hairpin occupies less than a 10th of the sphere volume. Our calculations show that the emergence of substantial structure in the denatured state of proteins in inert pores is a consequence of confinement. In contrast, the structure of the bulk denatured state ensemble depends dramatically on the extent of denaturation.
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