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Titolo:
Studying excited states of proteins by NMR spectroscopy
Autore:
Mulder, FAA; Mittermaier, A; 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:
NATURE STRUCTURAL BIOLOGY
fascicolo: 11, volume: 8, anno: 2001,
pagine: 932 - 935
SICI:
1072-8368(200111)8:11<932:SESOPB>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACID-BINDING PROTEIN; T4 LYSOZYME; CHEMICAL-EXCHANGE; CAVITY; FLEXIBILITY; DEPENDENCE; MUTANT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
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., "Studying excited states of proteins by NMR spectroscopy", NAT ST BIOL, 8(11), 2001, pp. 932-935

Abstract

Protein structure is inherently dynamic, with function often predicated onexcursions from low to higher energy conformations. For example, X-ray studies of a cavity mutant of T4 lysozyme, L99A, show that the cavity is sterically inaccessible to ligand, yet the protein is able to bind substituted benzenes rapidly. We have used novel relaxation dispersion NMR techniques tokinetically and thermodynamically characterize a transition between a highly populated (97%, 25 degreesC) ground state conformation and an excited state that is 2.0 kcal mol(-1) higher in free energy. A temperature-dependentstudy of the rates of interconversion between ground and excited states allows the separation of the free energy change into enthalpic (DeltaH = 7.1 kcal mol(-1)) and entropic (T DeltaS = 5.1 kcal mol(-1), 25 degreesC) components. The residues involved cluster about the cavity providing evidence that the excited state facilitates ligand entry.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/06/20 alle ore 01:58:13