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Titolo:
Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering
Autore:
Pollack, L; Tate, MW; Darnton, NC; Knight, JB; Gruner, SM; Eaton, WA; Austin, RH;
Indirizzi:
Cornell Univ, Atom & Solid State Phys Lab, Ithaca, NY 14853 USA Cornell Univ Ithaca NY USA 14853 lid State Phys Lab, Ithaca, NY 14853 USA Princeton Univ, Dept Phys, Princeton, NJ 08544 USA Princeton Univ Princeton NJ USA 08544 Dept Phys, Princeton, NJ 08544 USA NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA NIDDKD Bethesda MD USA20892 , Chem Phys Lab, NIH, Bethesda, MD 20892 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 18, volume: 96, anno: 1999,
pagine: 10115 - 10117
SICI:
0027-8424(19990831)96:18<10115:COTDSO>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYTOCHROME-C; LANDSCAPE PERSPECTIVE; KINETICS; INTERMEDIATE; LIGANDS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Pollack, L Cornell Univ, Atom & Solid State Phys Lab, Ithaca, NY 14853 USACornell Univ Ithaca NY USA 14853 hys Lab, Ithaca, NY 14853 USA
Citazione:
L. Pollack et al., "Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering", P NAS US, 96(18), 1999, pp. 10115-10117

Abstract

Time-resolved small-angle x-ray scattering was used to measure the radius of gyration of cytochrome c after initiation of folding by a pH jump. Submillisecond time resolution was obtained with a microfabricated diffusional mixer and synchrotron radiation. The results show that the protein first collapses to compact denatured structures before folding very fast to the native state.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 14:53:44