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Título

Detecting selection for negative design in proteins through an improved model of the misfolded state

Autor Minning, Jonas; Porto, Markus; Bastolla, Ugo
Palabras clave Negative design
Protein folding
Misfolding
Fecha de publicación 2013
EditorWiley-Liss
Citación Proteins: Structure, Function and Genetics 81: 1102- 1112 (2013)
ResumenProteins that need to be structured in their native state must be stable both against the unfolded ensemble and against incorrectly folded (misfolded) conformations with low free energy. Positive design targets the first type of stability by strengthening native interactions. The second type of stability is achieved by destabilizing interactions that occur frequently in the misfolded ensemble, a strategy called negative design. Here, we investigate negative design adopting a statistical mechanical model of the misfolded ensemble, which improves the usual Gaussian approximation by taking into account the third moment of the energy distribution and contact correlations. Applying this model, we detect and quantify selection for negative design in most natural proteins, and we analytically design protein sequences that are stable both against unfolding and against misfolding. © 2013 Wiley Periodicals, Inc.
URI http://hdl.handle.net/10261/95768
DOI10.1002/prot.24244
Identificadoresdoi: 10.1002/prot.24244
issn: 0887-3585
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