| Designing misfolded proteins by energy landscaping. | |
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MedLine Citation:
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PMID: 21158416 Owner: NLM Status: In-Process |
Abstract/OtherAbstract:
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Conformational fluctuations in the native state ensemble enhance the complexity in designing de novo protein sequences that may fold correctly into a desired target structure. In this work, the results of a self-consistent mean field theory are applied to a cubic lattice model of proteins and real nonhomologous proteins to assess the designability of folded, misfolded, and unfolded conformations. This theory, for the first time, accounts for the properties of misfolded sequences in terms of a generalized foldability criterion and characterizes the topography of the sequence energy landscape in terms of folded, misfolded, and unfolded ensemble of conformations. For a given foldability criterion, the folded, misfolded, and unfolded conformations may be distinctly classified by tuning the energy variance of the native state ensemble. This implies a promising route to de novo protein design and provides useful insights into understanding the impact of conformational similarity/diversity on the folding-misfolding-unfolding transition. |
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Authors:
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Arnab Bhattacherjee; Parbati Biswas |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-12-15 |
Journal Detail:
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Title: The journal of physical chemistry. B Volume: 115 ISSN: 1520-5207 ISO Abbreviation: J Phys Chem B Publication Date: 2011 Jan |
Date Detail:
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Created Date: 2011-01-06 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101157530 Medline TA: J Phys Chem B Country: United States |
Other Details:
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Languages: eng Pagination: 113-9 Citation Subset: IM |
Affiliation:
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Department of Chemistry, University of Delhi, Delhi-110007. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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