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Titolo:
Molecular confinement influences protein structure and enhances thermal protein stability
Autore:
Eggers, DK; Valentine, JS;
Indirizzi:
Univ Calif Los Angeles, Dept Biochem & Chem, Los Angeles, CA 90095 USA Univ Calif Los Angeles Los Angeles CA USA 90095 Los Angeles, CA 90095 USA
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 2, volume: 10, anno: 2001,
pagine: 250 - 261
SICI:
0961-8368(200102)10:2<250:MCIPSA>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
GEL SILICA GLASS; MACROMOLECULAR STRUCTURE; CARBONIC-ANHYDRASE; ALPHA-LACTALBUMIN; EXCLUDED-VOLUME; BETA-LACTOGLOBULIN; WATER; ENCAPSULATION; DETERMINANT; REACTIVITY;
Keywords:
protein folding; macromolecular crowding; sol-gel glass; circular dichroism; apomyoglobin; Hofmeister effect;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Eggers, DK Univ Calif Los Angeles, Dept Biochem & Chem, Los Angeles, CA 90095 USA Univ Calif Los Angeles Los Angeles CA USA 90095 , CA 90095 USA
Citazione:
D.K. Eggers e J.S. Valentine, "Molecular confinement influences protein structure and enhances thermal protein stability", PROTEIN SCI, 10(2), 2001, pp. 250-261

Abstract

The sol-gel method of encapsulating proteins in a silica matrix was investigated as a potential experimental system for testing the effects of molecular confinement on the structure and stability of proteins. We demonstrate that silica entrapment (1) is fully compatible with structure analysis by circular dichroism, (2) allows conformational studies in contact with solvents that would otherwise promote aggregation in solution, and (3) generally enhances thermal protein stability. Lysozyme, oc-lactalbumin, and metmyoglobin retained native-like solution structures following sol-gel encapsulation, but apomyoglobin was found to be largely unfolded within the silica matrix under control buffer conditions. The secondary structure of encapsulatedapomyoglobin was unaltered by changes in pH and ionic strength of KCl. Intriguingly, the addition of other neutral salts resulted in an increase in the cr-helical content of encapsulated apomyoglobin in accordance with the Hofmeister ion series. We hypothesize that protein conformation is influenced directly by the properties of confined water in the pores of the silica. Further work is needed to differentiate the steric effects of the silica matrix from the solvent effects of confined water on protein structure and todetermine the extent to which this experimental system mimics the effects of crowding and confinement on the function of macromolecules in vivo.

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Documento generato il 13/07/20 alle ore 07:14:53