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Assessing protein disorder and induced folding
Author(s) -
ReceveurBréchot Véronique,
Bourhis JeanMarie,
Uversky Vladimir N.,
Canard Bruno,
Longhi Sonia
Publication year - 2005
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20750
Subject(s) - intrinsically disordered proteins , folding (dsp implementation) , protein folding , function (biology) , residual , computer science , computational biology , chemistry , biology , biophysics , evolutionary biology , algorithm , biochemistry , engineering , electrical engineering
Intrinsically disordered proteins (IDPs) defy the structure–function paradigm as they fulfill essential biological functions while lacking well‐defined secondary and tertiary structures. Conformational and spectroscopic analyses showed that IDPs do not constitute a uniform family, and can be divided into subfamilies as a function of their residual structure content. Residual intramolecular interactions are thought to facilitate binding to a partner and then induced folding. Comprehensive information about experimental approaches to investigate structural disorder and induced folding is still scarce. We herein provide hints to readily recognize features typical of intrinsic disorder and review the principal techniques to assess structural disorder and induced folding. We describe their theoretical principles and discuss their respective advantages and limitations. Finally, we point out the necessity of using different approaches and show how information can be broadened by the use of multiples techniques. Proteins 2006. © 2005 Wiley‐Liss, Inc.