期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 103, 期 27, 页码 10254-10258出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0510110103
关键词
protein folding; topological frustration; two state; homologous; minimalist model
资金
- NIGMS NIH HHS [GM54038, F31 GM070412, 1-F31-GM070412-01, R29 GM054038, R01 GM054038] Funding Source: Medline
In general, the energy landscapes of real proteins are sufficiently well designed that the depths of local energetic minima are small compared with the global bias of the native state. Because of the funneled nature of energy landscapes, models that lack energetic frustration have been able to capture the main structural features of the transition states and intermediates found in experimental studies of both small and large proteins. In this study we ask: Are the experimental differences in folding mechanisms among members of a particular structural family due to local topological constraints that deviate from the tertiary fold common to the family? The beta-trefoil structural family members IL-1 beta, hisactophilin, and acidic/basic FGFs were chosen to address this question. It has been observed that the topological landscape of the beta-trefoils allows for the population of diverse, geometrically disconnected routes that provide energetically similar but structurally distinct ways for this family to fold. Small changes in topology or energetics can alter the preferred route. Taken together, these results indicate that the global fold of the beta-trefoil family determines the energy landscape but that the routes accessed on that landscape might differ as a result of functional requirements of the individual family members.
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