Characterizing weak protein–protein complexes by NMR residual dipolar couplings

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)

University of Kent Author Information

Ortega-Roldan, Jose L..

Creator's ORCID:	https://orcid.org/0000-0002-6316-4390
CReDIT Contributor Roles:

Depositors only (login required):

Altmetric

Download Statistics

Total unique views for this document in KAR since July 2020. For more details click on the image.