A comprehensive library of blocked dipeptides reveals intrinsic backbone conformational propensities of unfolded proteins

Despite prolonged scientific efforts to elucidate the intrinsic peptide backbone preferences of amino‐acids based on understanding of intermolecular forces, many open questions remain, particularly concerning neighboring peptide interaction effects on the backbone conformational distribution of shor...

Full description

Saved in:
Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2012-04, Vol.80 (4), p.977-990
Main Authors: Oh, Kwang-Im, Lee, Kyung-Koo, Park, Eun-Kyung, Jung, Youngae, Hwang, Geum-Sook, Cho, Minhaeng
Format: Article
Language:English
Subjects:
Amino Acids - chemistry
blocked dipeptide
Circular Dichroism
Dipeptides - chemical synthesis
Dipeptides - chemistry
Hydrogen Bonding
Magnetic Resonance Spectroscopy
peptide conformation
Peptide Library
polyproline II
Protein Conformation
Protein Stability
Protein Unfolding
Solvents - chemistry
Static Electricity
unfolded protein structure
Water - chemistry
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Despite prolonged scientific efforts to elucidate the intrinsic peptide backbone preferences of amino‐acids based on understanding of intermolecular forces, many open questions remain, particularly concerning neighboring peptide interaction effects on the backbone conformational distribution of short peptides and unfolded proteins. Here, we show that spectroscopic studies of a complete library of 400 dipeptides reveal that, irrespective of side‐chain properties, the backbone conformation distribution is narrow and they adopt polyproline II and β‐strand, indicating the importance of backbone peptide solvation and electronic effects. By directly comparing the dipeptide circular dichroism and NMR results with those of unfolded proteins, the comprehensive dipeptides form a complete set of structural motifs of unfolded proteins. We thus anticipate that the present dipeptide library with spectroscopic data can serve as a useful database for understanding the nature of unfolded protein structures and for further refinements of molecular mechanical parameters. Proteins 2011; © 2011 Wiley Periodicals, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.24000