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Neighboring Residue Effects in Terminally Blocked Dipeptides: Implications for Residual Secondary Structures in Intrinsically Unfolded/Disordered Proteins
Author(s) -
Jung YoungSang,
Oh KwangIm,
Hwang GeumSook,
Cho Minhaeng
Publication year - 2014
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.22285
Subject(s) - chemical shift , chemistry , random coil , residue (chemistry) , protein secondary structure , intrinsically disordered proteins , nuclear magnetic resonance spectroscopy , side chain , crystallography , chemical modification , hydrogen bond , molecule , stereochemistry , circular dichroism , organic chemistry , biochemistry , polymer
For nuclear magnetic resonance (NMR)‐based protein structure determinations, the random coil chemical shifts are very important because the secondary and tertiary protein structure predictions become possible by examining deviations of measured chemical shifts from those reference chemical shift values. In addition, neighboring residue effects on chemical shifts and J ‐coupling constants are crucial in understanding the nature of conformational propensities exhibited by unfolded or intrinsically disordered proteins. We recently reported the 1D NMR results for a complete set of terminally blocked dipeptides (Oh KI, Jung YS, Hwang GS, Cho M. J Biomol NMR 2012;53:25–41), but the NMR resonance assignments were not possible so that the average chemical shifts and J ‐coupling constants were only considered. In the present work, to thoroughly investigate the neighboring residue effects and random coil chemical shifts we extend the previous studies with 2D NMR, and measured all the 3 J HNHα values and H α and H N chemical shifts of the same set of terminally blocked dipeptides that are free from structural effects like secondary structure, hydrogen‐bond, long‐range backbone, and side‐chain interactions. In particular, the preceding and following residue effects on amino‐acid backbone conformational propensities are revealed and directly compared with previous works on either short peptides or empirical chemical shift database. Chirality 26:443‐452, 2014 . © 2014 Wiley Periodicals, Inc.