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PMID: 11061227 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView.

Journal of biomolecular NMR ·Vol. 18 ·No. 1 ·2000-09-00 ·Pages 43-8

Schwarzinger S, Kroon GJ, Foss TR, Wright PE, Dyson HJ

Abstract

Studies of proteins unfolded in acid or chemical denaturant can help in unraveling events during the earliest phases of protein folding. In order for meaningful comparisons to be made of residual structure in unfolded states, it is necessary to use random coil chemical shifts that are valid for the experimental system under study. We present a set of random coil chemical shifts obtained for model peptides under experimental conditions used in studies of denatured proteins. This new set, together with previously published data sets, has been incorporated into a software interface for NMRView, allowing selection of the random coil data set that fits the experimental conditions best.

MeSH Terms
Data Display Databases, Factual Nuclear Magnetic Resonance, Biomolecular/methods Oligopeptides/chemistry Protein Denaturation Protein Structure, Secondary/drug effects Urea/pharmacology
Chemicals
Oligopeptides Urea
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Schwarzinger S
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Kroon G J
Foss T R
Wright P E
Dyson H J
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Article Info
Journal
Journal of biomolecular NMR
Abbr.
J Biomol NMR
ISSN
0925-2738
DOI
10.1023/a:1008386816521
Published
2000-09-00
Pages
43-8
Language
English
Region
Netherlands
NLM ID
9110829
Subset
IM
Grants
NIGMS NIH HHS · GM57374 · United States
Corrections
ErratumIn
-
External Links
PubMed source DOI: 10.1023/a:1008386816521 View journal details
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