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Conformational and connotational heterogeneity: A surprising relationship between protein structural flexibility and puns
ABSTRACT Protein structures are often thought of as static objects, and indeed, the bulk of a protein's sequence forms α‐helices, β‐sheets, and other generally well‐ordered substructures. These portions of the molecule pre‐pay the entropic price of maintaining a globally unique fold, freeing ot...
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Published in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2015-05, Vol.83 (5), p.797-798 |
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Main Author: | |
Format: | Article |
Language: | English |
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Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | ABSTRACT
Protein structures are often thought of as static objects, and indeed, the bulk of a protein's sequence forms α‐helices, β‐sheets, and other generally well‐ordered substructures. These portions of the molecule pre‐pay the entropic price of maintaining a globally unique fold, freeing other regions to adopt multiple alternative conformations. In many cases, this localized flexibility is biologically interesting: it may be important for catalytic turnover or for conformational selection before forming an intermolecular complex, for example. Similarly, most of written language is carefully tuned to avoid ambiguity and convey a singular meaning, a cohesive message. This linguistic scaffolding in some sense pre‐pays a rhetorical price, paving the way for punctuated instances in which a given word or phrase can simultaneously adopt multiple alternative connotations—in other words, for puns. Proteins 2015; 83:797–798. © 2015 Wiley Periodicals, Inc. |
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ISSN: | 0887-3585 1097-0134 |
DOI: | 10.1002/prot.24765 |