Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 80, Issue 4, Pages 977-990Publisher
WILEY
DOI: 10.1002/prot.24000
Keywords
peptide conformation; blocked dipeptide; polyproline II; unfolded protein structure
Categories
Funding
- Ministry of Education, Science and Technology, National Research Foundation (NRF), Korea [20090078897]
- Korea Basic Science Institute (KBSI) [T31401]
- Korea University
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available