NDLI: Polyproline II helical structure in protein unfolded states: lysine peptides revisited.

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Polyproline II helical structure in protein unfolded states: lysine peptides revisited.

Free energies of protein decoys provide insight into determinants of protein stability.

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Polyproline II helical structure in protein unfolded states: lysine peptides revisited.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Rucker, Adam L. Creamer, Trevor P.
Description	Country affiliation: United States Author Affiliation: Rucker AL ( Center for Structural Biology, Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky 40536-0298, USA.)
Abstract	The left-handed polyproline II (PPII) helix gives rise to a circular dichroism spectrum that is remarkably similar to that of unfolded proteins. This similarity has been used as the basis for the hypothesis that unfolded proteins possess considerable PPII helical content. It has long been known that homopolymers of lysine adopt the PPII helical conformation at neutral pH, presumably a result of electrostatic repulsion between side chains. It is shown here that a seven-residue lysine peptide also adopts the PPII conformation. In contrast with homopolymers of lysine, this short peptide is shown to retain PPII helical character under conditions in which side-chain charges are heavily screened or even neutralized. The most plausible explanation for these observations is that the peptide backbone favors the PPII conformation to maximize favorable interactions with solvent. These data are evidence that unfolded proteins do indeed possess PPII content, indicating that the ensemble of unfolded states is significantly smaller than is commonly assumed.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	4
Volume Number	11
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2002-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Lysine Chemistry Peptides Circular Dichroism Hydrogen Bonding Protein Conformation Protein Folding Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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