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

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 id...

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Publisher copy:
10.1007/s10858-004-7912-6

Authors


Deschamps, ML More by this author
Campbell, ID More by this author
Journal:
Journal of biomolecular NMR
Volume:
31
Issue:
2
Pages:
155-160
Publication date:
2005-02-05
DOI:
EISSN:
1573-5001
ISSN:
0925-2738
URN:
uuid:412d0095-6de4-42e7-8072-655072568407
Source identifiers:
246420
Local pid:
pubs:246420

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