期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 105, 期 23, 页码 8004-8007出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0708411105
关键词
protein folding; all-atom simulation; folding mechanism; chameleon segment; nonnative intermediates
资金
- NIGMS NIH HHS [GM62838, R01 GM062838] Funding Source: Medline
Protein structures often feature beta-sheets in which adjacent beta-strands have large sequence separation. How the folding process orchestrates the formation and correct arrangement of these strands is not comprehensively understood. Particularly. challenging are proteins in which beta-strands at the N and C termini are neighbors in a beta-sheet. The N-terminal beta-strand is synthesized early on, but it can not bind to the C terminus before the chain is fully synthesized. During this time, there is a danger that the beta-strand at the N terminus interacts with nearby molecules, leading to potentially harmful aggregates of incompletely folded proteins. Simulations of the C-terminal fragment of Top7 show that this risk of misfolding and aggregation can be avoided by a caching mechanism that relies on the chameleon behavior of certain segments.
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