We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView.
- Authors
Schwarzinger, Stephan; Kroon, Gerard J.A.; Foss, Ted R.; Wright, Peter E.; Dyson, H. Jane
- 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.
- Subjects
PROTEIN folding; PROTEIN conformation; NUCLEAR magnetic resonance; PEPTIDES; PROTEINS; NUCLEAR induction
- Publication
Journal of Biomolecular NMR, 2000, Vol 18, Issue 1, p43
- ISSN
0925-2738
- Publication type
Article
- DOI
10.1023/A:1008386816521