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The structure of “unstructured” regions in peptides and proteins: Role of the polyproline II helix in protein folding and recognition *
Author(s) -
Rath Arianna,
Davidson Alan R.,
Deber Charles M.
Publication year - 2005
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20227
Subject(s) - polyproline helix , chemistry , protein folding , peptide , biophysics , sh3 domain , helix (gastropod) , protein structure , folding (dsp implementation) , signal transduction , biochemistry , proto oncogene tyrosine protein kinase src , biology , ecology , snail , electrical engineering , engineering
Classical descriptions of the three‐dimensional shapes of proteins usually invoke three main structures: α‐helix, β‐sheet, and β‐turn. More recently, the polyproline II (PPII) structure has been implicated in diverse biological activities including signal transduction, transcription, cell motility, and immune response. Concurrently, evidence is accumulating that PPII structure has a significant role in the unfolded states of proteins. In this article, we connect the structural properties of PPII helices to their roles in protein recognition and protein unfolded states. The properties unique to the PPII conformation are linked to the exploitation of this structure for the molecular recognition of proteins, using peptide ligands of the Src homology 3 (SH3) domain as an example. The evidence supporting a role for PPII conformation in protein‐unfolded states is also presented in the context of the forces that may stabilize the PPII conformation in unfolded polypeptides. © Wiley Periodicals Inc. Biopolymers (Pept Sci), 2005