- Abstract:
-
Values of S2CH and S2NH order parameters derived from NMR relaxation measurements on proteins cannot straightforwardly be used to determine protein structure, because they cannot be related to a single protein structure, but are defined in terms of an average over a conformational ensemble. MD simulation can generate a conformational ensemble and thus be used to restrain S2CH and S2NH order parameters towards experimentally derived target values S2CH(exp) and S2NH(exp). Application of S2CH an...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Files:
-
- Publisher copy:
- 10.1002/cbic.202000674
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- Publisher:
- Wiley Publisher's website
- Journal:
- Chembiochem Journal website
- Publication date:
- 2020-11-04
- Acceptance date:
- 2020-11-02
- DOI:
- EISSN:
-
1439-7633
- ISSN:
-
1439-4227
- Pmid:
-
33146424
- Pubs id:
-
1140906
- Local pid:
- pubs:1140906
- Language:
- English
- Keywords:
- Format:
- Print-Electronic
- Copyright holder:
- Wiley
- Copyright date:
- 2020
- Rights statement:
- © 2020 Wiley‐VCH GmbH. This paper is open access under a Creative Commons Attribution (CC-BY 4.0) licence.
- License:
- CC Attribution (CC BY)
Journal article
On the use of side-chain NMR relaxation data to derive structural and dynamical information on proteins: A case study using Hen Lysozyme
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