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Titolo:
Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: A F-19-NMR study
Autore:
Bai, P; Luo, L; Peng, ZY;
Indirizzi:
Univ Connecticut, Ctr Hlth, Dept Biochem, Farmington, CT 06032 USA Univ Connecticut Farmington CT USA 06032 iochem, Farmington, CT 06032 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 2, volume: 39, anno: 2000,
pagine: 372 - 380
SICI:
0006-2960(20000118)39:2<372:SCAADI>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; D-LACTATE DEHYDROGENASE; ESCHERICHIA-COLI; PROTEIN-STRUCTURE; FOLDING INTERMEDIATE; 3-STATE DENATURATION; HYDROGEN-EXCHANGE; NMR-SPECTROSCOPY; HYDROPHOBIC CORE; STOPPED-FLOW;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
62
Recensione:
Indirizzi per estratti:
Indirizzo: Peng, ZY Univ Connecticut, Ctr Hlth, Dept Biochem, 263 Farmington Ave,MC-3305, Farmington, CT 06032 USA Univ Connecticut 263 Farmington Ave,MC-3305 Farmington CT USA 06032
Citazione:
P. Bai et al., "Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: A F-19-NMR study", BIOCHEM, 39(2), 2000, pp. 372-380

Abstract

The molten globule state of alpha-lactalbumin (alpha-LA) has been considered a prototype of partially folded proteins. Despite the importance of molten globules in understanding the mechanisms of protein folding and its relevance to some biological phenomena, site-specific information on the structure and dynamics of a molten globule is limited, largely because of the high conformational flexibility and heterogeneity. Here, we use selective isotope labeling and F-19 NMR to investigate the solvent accessibility and side-chain dynamics of aromatic residues in the molten globule of alpha-LA. Comparison of these proper-ties with those of the native and unfolded protein indicates that the alpha-LA molten globule is highly heterogeneous; each residue has its unique solvent accessibility and motional environment. Many aromatic residues normally buried in the interior of native alpha-LA remain significantly buried in the molten globule and the side-chain dynamics of these residues are highly restricted. Our results suggest that hydrophobic and van der Waals interactions mediated by the inaccessible surface area could be sufficient to account for all the stability of the alpha-LA molten globule, which is approximately 50% of the value for the native protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 15:47:19