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Titolo:
Measurement of slow (mu s-ms) time scale dynamics in protein side chains by N-15 relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme
Autore:
Mulder, FAA; Skrynnikov, NR; 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: 5, volume: 123, anno: 2001,
pagine: 967 - 975
SICI:
0002-7863(20010207)123:5<967:MOS(ST>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
HETERONUCLEAR TRANSVERSE RELAXATION; COUPLED SPIN SYSTEMS; CHEMICAL-EXCHANGE; CROSS-CORRELATION; BACKBONE DYNAMICS; DOMAIN; RESONANCE; MOTIONS; SPECTRA; MICROSECOND;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
68
Recensione:
Indirizzi per estratti:
Indirizzo: Kay, LE Univ Toronto, Prot Engn Network Ctr Excellence, 100 Coll St, Toronto, ON M5S 1A8, Canada Univ Toronto 100 Coll St Toronto ON Canada M5S 1A8 M5S 1A8, Canada
Citazione:
F.A.A. Mulder et al., "Measurement of slow (mu s-ms) time scale dynamics in protein side chains by N-15 relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme", J AM CHEM S, 123(5), 2001, pp. 967-975

Abstract

A new NMR experiment is presented for the measurement of mus-ms time scaledynamics of Asn and Gin side chains in proteins. Exchange contributions tothe N-15 line widths of side chain residues are determined via a relaxation dispersion experiment in which the effective nitrogen transverse relaxation rate is measured as a function of the number of refocusing pulses in constant-time, variable spacing CPMG intervals. The evolution of magnetizationfrom scalar couplings and dipole-dipole cross-correlations, which has limited studies of exchange in multi-spin systems in the past, does not affect the extraction of accurate exchange parameters from relaxation profiles of NH2 groups obtained in the present experiment. The utility of the method isdemonstrated with an application to a Leu --> Ala cavity mutant of T4 lysozyme, L99A. II is shown that many of the side chain amide groups of Asn andGin residues in the C-terminal domain of the protein are affected by a chemical exchange process which may be important in facilitating the rapid binding of hydrophobic ligands to the cavity.

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Documento generato il 11/07/20 alle ore 04:40:34