Disorder and order in unfolded and disordered peptides and proteins: A view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains-Reference-Cited by-同舟云学术

Disorder and order in unfolded and disordered peptides and proteins: A view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains

Published:2013-02-27 Issue:6 Volume:81 Page:955-967
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Schweitzer-Stenner Reinhard,Hagarman Andrew,Toal Siobhan,Mathieu Daniel,Schwalbe Harald

Funder

NSF

REU

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.24225/fullpdf

Reference63 articles.

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4. Further evidence for the absence of polyrpoline II stretch in the XAO peptide;Makowska;Biophys J,2007

5. Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins;Makowska;Proc Natl Acad Sci USA,2006

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