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

Authors
Oh, Kwang-ImLee, Kyung-KooPark, Eun-KyungJung, YoungaeHwang, Geum-SookCho, Minhaeng
Issue Date
4월-2012
Publisher
WILEY
Keywords
peptide conformation; blocked dipeptide; polyproline II; unfolded protein structure
Citation
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v.80, no.4, pp.977 - 990
Indexed
SCIE
SCOPUS
Journal Title
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume
80
Number
4
Start Page
977
End Page
990
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/108852
DOI
10.1002/prot.24000
ISSN
0887-3585
Abstract
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 (-) beta 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; (c) 2011 Wiley Periodicals, Inc.
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