Jensen, Malene Ringkjøbing, Ortega-Roldan, Jose L., Salmon, Loïc, van Nuland, Nico, Blackledge, Martin (2011) Characterizing weak protein–protein complexes by NMR residual dipolar couplings. European Biophysics Journal, 40 (12). pp. 1371-1381. ISSN 0175-7571. E-ISSN 1432-1017. (doi:10.1007/s00249-011-0720-5) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:62502)
PDF
Publisher pdf
Language: English Restricted to Repository staff only |
|
|
|
Official URL: https://doi.org/10.1007/s00249-011-0720-5 |
Abstract
Protein–protein interactions occur with a wide range of affinities from tight complexes characterized by femtomolar dissociation constants to weak, and more transient, complexes of millimolar affinity. Many of the weak and transiently formed protein–protein complexes have escaped characterization due to the difficulties in obtaining experimental parameters that report on the complexes alone without contributions from the unbound, free proteins. Here, we review recent developments for characterizing the structures of weak protein–protein complexes using nuclear magnetic resonance spectroscopy with special emphasis on the utility of residual dipolar couplings.
Item Type: | Article |
---|---|
DOI/Identification number: | 10.1007/s00249-011-0720-5 |
Uncontrolled keywords: | NMR, Interaction, Protein, Dynamics, Structure, Complex |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Jose Ortega Roldan |
Date Deposited: | 31 Jul 2017 15:11 UTC |
Last Modified: | 16 Nov 2021 10:24 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/62502 (The current URI for this page, for reference purposes) |
- Export to:
- RefWorks
- EPrints3 XML
- BibTeX
- CSV
- Depositors only (login required):