Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
CRYSTALLIZATION OF MONOACYLATED PROTEINS - INFLUENCE OF ACYL-CHAIN LENGTH
Autore:
ROY MO; UPPENBERG J; ROBERT S; BOYER M; CHOPINEAU J; JULLIEN M;
Indirizzi:
UNIV MONTPELLIER 2,FAC PHARM,CTR BIOCHIM STRUCT,CNRS,UMR C9955,INSERM,U414 F-34060 MONTPELLIER FRANCE UNIV MONTPELLIER 2,FAC PHARM,CTR BIOCHIM STRUCT,CNRS,UMR C9955,INSERM,U414 F-34060 MONTPELLIER FRANCE UNIV TECHNOL COMPIEGNE,TECHNOL ENZYMAT LAB,UPRES CNRS A6022 F-60205 COMPIEGNE FRANCE
Titolo Testata:
European biophysics journal
fascicolo: 2, volume: 26, anno: 1997,
pagine: 155 - 162
SICI:
0175-7571(1997)26:2<155:COMP-I>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELASTIC LIGHT-SCATTERING; RIBONUCLEASE-A; CRYSTAL FORMS; RESOLUTION; PEPTIDES; RNASE;
Keywords:
ACYLATION; RIBONUCLEASE A; SELF-ASSOCIATION; PROTEIN CRYSTALLOGRAPHY; DYNAMIC LIGHT SCATTERING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
M.O. Roy et al., "CRYSTALLIZATION OF MONOACYLATED PROTEINS - INFLUENCE OF ACYL-CHAIN LENGTH", European biophysics journal, 26(2), 1997, pp. 155-162

Abstract

The crystallization of monoacylated proteins has been investigated using a model system. Acylated derivatives of bovine pancreatic ribonuclease A, differing in their acyl chain lengths (10 to 16 carbon atoms),have been prepared using reverse micelles as microreactors. With one fatty acid moiety per polypeptide chain, covalently attached to the NH2 terminus of the protein, all the modified proteins have similar enzymatic activity and hydrodynamic radius as the native protein. Only thecaprylated derivative can give crystals which diffract to high resolution. The resolved structure indicates that: (i) the protein folding is not modified by the chemical modification, (ii) the capryl moiety isnot buried within the molecule but available for external interactions. Dynamic light scattering experiments on concentrated solutions showthat protein-protein interactions are dependent on acyl chain length. Proteins with the longest attached chains (14 and 16 carbon atoms) tend to self-associate through acyl group interactions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 12:54:06