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Titolo:
Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme
Autore:
Skrynnikov, NR; Mulder, FAA; Hon, B; Dahlquist, FW; Kay, LE;
Indirizzi:
Univ Toronto, Prot Engn Network Ctr Excellence, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 lence, Toronto, ON M5S 1A8, Canada Univ Toronto, Dept Med Genet, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 Genet, Toronto, ON M5S 1A8, Canada Univ Toronto, Dept Biochem & Chem, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 Chem, Toronto, ON M5S 1A8, Canada Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA Univ Oregon Eugene OR USA 97403 egon, Inst Mol Biol, Eugene, OR 97403 USA Univ Oregon, Dept Chem, Eugene, OR 97403 USA Univ Oregon Eugene OR USA 97403 v Oregon, Dept Chem, Eugene, OR 97403 USA
Titolo Testata:
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
fascicolo: 19, volume: 123, anno: 2001,
pagine: 4556 - 4566
SICI:
0002-7863(20010516)123:19<4556:PSTSDA>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
MODEL-FREE APPROACH; HETERONUCLEAR TRANSVERSE RELAXATION; MAGNETIC-RESONANCE RELAXATION; SPIN SYSTEMS; H-2-LABELED PROTEINS; CROSS-CORRELATION; C-13 RELAXATION; SPECTROSCOPY; EXCHANGE; DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Kay, LE Univ Toronto, Prot Engn Network Ctr Excellence, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 oronto, ON M5S 1A8, Canada
Citazione:
N.R. Skrynnikov et al., "Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme", J AM CHEM S, 123(19), 2001, pp. 4556-4566

Abstract

A relaxation dispersion-based NMR experiment is presented for the measurement and quantitation of mus-ms dynamic processes at methyl side-chain positions in proteins. The experiment measures the exchange contribution to the C-13 line widths of methyl groups using a constant-time CPMG scheme. The effects of cross-correlated spin relaxation between dipole-dipole and dipole-CSA interactions as well as the effects of scalar coupling responsible for mixing of magnetization modes during the course of the experiment have beeninvestigated in detail both theoretically and through simulations. It is shown that the complex relaxation properties of the methyl spin system do not complicate extraction of accurate exchange parameters as long as care is taken to ensure that appropriate magnetization modes are interchanged in the middle of the constant-time CPMG period. An application involving the measurement of relaxation dispersion profiles of methionine residues in a Leu99Ala substitution of T4 lysozyme is presented. All of the methionine residues are sensitive to an exchange event with a rate on the order of 1200 s(-1) at 20 degreesC that may be linked to a process in which hydrophobic ligands are able to rapidly bind to the cavity that is present in this mutant.

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Documento generato il 09/07/20 alle ore 01:42:39