Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 50, Pages 19819-19824Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0709915104
Keywords
protein folding; protein function; energy landscape
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Funding
- NIGMS NIH HHS [R01GM44557, P01GM071862, R01 GM044557, P01 GM071862] Funding Source: Medline
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We propose a method of quantifying the degree of frustration manifested by spatially local interactions in protein biomolecules. This method of localization smoothly generalizes the global criterion for an energy landscape to be funneled to the native state, which is in keeping with the principle of minimal frustration. A survey of the structural database shows that natural proteins are multiply connected by a web of local interactions that are individually minimally frustrated. In contrast, highly frustrated interactions are found clustered on the surface, often near binding sites. These binding sites become less frustrated upon complex formation.
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