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Titolo:
Preorganized secondary structure as an important determinant of fast protein folding
Autore:
Myers, JK; Oas, TG;
Indirizzi:
Duke Univ, Med Ctr, Dept Biochem, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 Med Ctr, Dept Biochem, Durham, NC 27710 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 6, volume: 8, anno: 2001,
pagine: 552 - 558
SICI:
1072-8368(200106)8:6<552:PSSAAI>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIFFUSION-COLLISION MODEL; SINGLE-DOMAIN PROTEINS; TRANSITION-STATE; LAMBDA-REPRESSOR; CONTACT ORDER; T4 LYSOZYME; KINETICS; PEPTIDE; INTERMEDIATE; DYNAMICS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Oas, TG Duke Univ, Med Ctr, Dept Biochem, Box 3711, Durham, NC 27710 USA Duke Univ Box 3711 Durham NC USA 27710 3711, Durham, NC 27710 USA
Citazione:
J.K. Myers e T.G. Oas, "Preorganized secondary structure as an important determinant of fast protein folding", NAT ST BIOL, 8(6), 2001, pp. 552-558

Abstract

The folding and unfolding kinetics of the B-domain of staphylococcal protein A, a small three-helix bundle protein, were probed by NMR. The lineshapeof a single histidine resonance was fit as a function of denaturant to give folding and unfolding rate constants. The B-domain folds extremely rapidly in a two-state manner, with a folding rate constant of 120,000 s(-1), making it one of the fastest-folding proteins known. Diffusion-collision theory predicts folding and unfolding rate constants that are in good agreement with the experimental values. The apparent rate constant as a function of denaturant ('chevron plot') is predicted within an order of magnitude. Our results are consistent with a model whereby fast-folding proteins utilize a diffusion-collision mechanism, with the preorganization of one or more elements of secondary structure in the unfolded protein.

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Documento generato il 04/04/20 alle ore 12:22:00