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Sequence-Dependent Correction of Random Coil NMR Chemical Shifts

Title data

Schwarzinger, Stephan ; Kroon, Gerard J. A. ; Foss, Ted R. ; Chung, John ; Wright, Peter E. ; Dyson, H. Jane:
Sequence-Dependent Correction of Random Coil NMR Chemical Shifts.
In: Journal of the American Chemical Society. Vol. 123 (March 2001) Issue 13 . - pp. 2970-2978.
ISSN 1520-5126
DOI: https://doi.org/10.1021/ja003760i

Abstract in another language

Random coil chemical shifts are commonly used to detect secondary structure elements in proteins in chemical shift index calculations. While this technique is very reliable for folded proteins, application to unfolded proteins reveals significant deviations from measured random coil shifts for certain nuclei. While some of these deviations can be ascribed to residual structure in the unfolded protein, others are clearly caused by local sequence effects. In particular, the amide nitrogen, amide proton, and carbonyl carbon chemical shifts are highly sensitive to the local amino acid sequence. We present a detailed, quantitative analysis of the effect of the 20 naturally occurring amino acids on the random coil shifts of 15NH, 1HN, and 13CO resonances of neighboring residues, utilizing complete resonance assignments for a set of five-residue peptides Ac-G-G-X-G-G-NH2. The work includes a validation of the concepts used to derive sequence-dependent correction factors for random coil chemical shifts, and a comprehensive tabulation of sequence-dependent correction factors that can be applied for amino acids up to two residues from a given position. This new set of correction factors will have important applications to folded proteins as well as to short, unstructured peptides and unfolded proteins.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Research Institutions
Research Institutions > Research Centres
Research Institutions > Research Centres > Nordbayerisches Zentrum für NMR-Spektroskopie - NMR-Zentrum
Result of work at the UBT: No
DDC Subjects: 500 Science > 500 Natural sciences
Date Deposited: 07 Aug 2019 08:40
Last Modified: 07 Aug 2019 08:40
URI: https://eref.uni-bayreuth.de/id/eprint/51781