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Titolo:
Protein dynamic studies move to a new time slot
Autore:
Cavanagh, J; Venters, RA;
Indirizzi:
N Carolina State Univ, Dept Mol & Struct Biochem, Raleigh, NC 27695 USA N Carolina State Univ Raleigh NC USA 27695 Biochem, Raleigh, NC 27695 USA Duke Univ, NMR Ctr, Durham, NC 27710 USA Duke Univ Durham NC USA 27710Duke Univ, NMR Ctr, Durham, NC 27710 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 11, volume: 8, anno: 2001,
pagine: 912 - 914
SICI:
1072-8368(200111)8:11<912:PDSMTA>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
T4 LYSOZYME; CHEMICAL-EXCHANGE; NMR-SPECTROSCOPY; HETERONUCLEAR CORRELATION; ORDER PARAMETERS; RELAXATION; BINDING; ENTROPY; CAVITY; RATES;
Tipo documento:
Editorial Material
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Cavanagh, J N Carolina State Univ, Dept Mol & Struct Biochem, Raleigh, NC 27695 USA N Carolina State Univ Raleigh NC USA 27695 eigh, NC 27695 USA
Citazione:
J. Cavanagh e R.A. Venters, "Protein dynamic studies move to a new time slot", NAT ST BIOL, 8(11), 2001, pp. 912-914

Abstract

Many proteins frequently undergo structural rearrangement to complete their functions. Ligand entry and binding are often associated with some degreeof localized disorder. Indeed, low populations of disordered excited states may help drive such processes. Characterization of these states is vital to understanding the mechanisms of many biological functions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/06/20 alle ore 01:08:54