| License: Creative Commons Attribution 4.0 PDF - Published Version (1MB) |
- URN to cite this document:
- urn:nbn:de:bvb:355-epub-447743
- DOI to cite this document:
- 10.5283/epub.44774
This publication is part of the DEAL contract with Springer.
Abstract
Proteins and nucleic acids are highly dynamic bio-molecules that can populate a variety of conformational states. NMR relaxation dispersion (RD) methods are uniquely suited to quantify the associated kinetic and thermodynamic parameters. Here, we present a consistent suite of F-19-based CPMG, on-resonance R-1 rho and off-resonance R-1 rho RD experiments. We validate these experiments by studying ...
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