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Titolo:
Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR
Autore:
Mulder, FAA; Hon, B; Muhandiram, DR; 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, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 ochem, Toronto, ON M5S 1A8, Canada Univ Toronto, Dept Chem, Toronto, ON M5S 1A8, Canada Univ Toronto TorontoON 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:
BIOCHEMISTRY
fascicolo: 41, volume: 39, anno: 2000,
pagine: 12614 - 12622
SICI:
0006-2960(20001017)39:41<12614:FALEIA>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
TIME-SCALE DYNAMICS; DNA-BINDING DOMAIN; BACKBONE DYNAMICS; BACTERIOPHAGE-T4 LYSOZYME; PROTEIN STABILITY; RELAXATION; N-15; ASSIGNMENTS; MOTIONS; CORE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
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., "Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR", BIOCHEM, 39(41), 2000, pp. 12614-12622

Abstract

The Leu99-->Ala mutant of T4 lysozyme contains a large internal cavity in the core of its C-terminal domain that is capable of reversibly binding small hydrophobic compounds. Although the cavity is completely buried, molecules such as benzene or xenon can exchange rapidly in and out. The dynamics of the unliganded protein have been compared to the wild-type protein by measuring the NMR spin relaxation rates of backbone amide and side chain methyl nuclei. Many residues surrounding the cavity were found to be affected bya chemical exchange process with a rate of 1500 +/- 200 s(-1), which is quenched upon addition of saturating amounts of the ligand xenon. The relationship between the structure, dynamics, and energetics of the T4 lysozyme mutant is discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 14:59:59