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

Michaël L Deschamps; Ewa S Pilka; Jennifer R Potts; Iain D Campbell; Jonathan Boyd

doi:10.1007/s10858-004-7912-6

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

Michaël L Deschamps, Ewa S Pilka, Jennifer R Potts, Iain D Campbell, Jonathan Boyd

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	155-60
Number of pages	6
Journal	JOURNAL OF BIOMOLECULAR NMR
Volume	31
Issue number	2
DOIs	https://doi.org/10.1007/s10858-004-7912-6
Publication status	Published - 2005

Keywords

Binding Sites
Free Radicals
Humans
Models, Molecular
Nitrogen
Nitrogen Oxides
Nuclear Magnetic Resonance, Biomolecular
Peptides
Protein Binding
Protein Structure, Tertiary
Proteins
Protons
Static Electricity

Access to Document

10.1007/s10858-004-7912-6

Cite this

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title = "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 identifying regions of the surface of the 4F1(5)F1 module pair from human fibronectin involved in peptide binding.",

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T1 - Probing protein-peptide binding surfaces using charged stable free radicals and transverse paramagnetic relaxation enhancement (PRE)

AU - Deschamps, Michaël L

AU - Pilka, Ewa S

AU - Potts, Jennifer R

AU - Campbell, Iain D

AU - Boyd, Jonathan

PY - 2005

Y1 - 2005

N2 - 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.

AB - 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.

KW - Binding Sites

KW - Free Radicals

KW - Humans

KW - Models, Molecular

KW - Nitrogen

KW - Nitrogen Oxides

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Peptides

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - Proteins

KW - Protons

KW - Static Electricity

U2 - 10.1007/s10858-004-7912-6

DO - 10.1007/s10858-004-7912-6

M3 - Article

C2 - 15772755

VL - 31

SP - 155

EP - 160

JO - JOURNAL OF BIOMOLECULAR NMR

JF - JOURNAL OF BIOMOLECULAR NMR

SN - 0925-2738

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