Format

Send to

Choose Destination
See comment in PubMed Commons below
J Biomol NMR. 2005 Feb;31(2):155-60.

Probing protein-peptide binding surfaces using charged stable free radicals and transverse paramagnetic relaxation enhancement (PRE).

Author information

1
Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, Oxford, UK. Michael.Deschamps@bioch.ox.ac.uk

Abstract

Nitroxide species, which have an unpaired electron localized on a nitrogen atom, can be useful as NMR probes to identify areas of the surface of a protein involved in the formation of a complex. The proximity of an electron spin leads to higher NMR relaxation rates for protein nuclei. If a protein-ligand complex is formed the radical is excluded from certain sites on the protein surface, protecting them from relaxation effects. We show here that charged nitroxide species can be helpful for identifying regions of the surface of the 4F1(5)F1 module pair from human fibronectin involved in peptide binding.

PMID:
15772755
DOI:
10.1007/s10858-004-7912-6
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Support Center