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Titolo:
Reversible, thermally induced domain unfolding in oligomeric proteins - Spectral and DSC measurements
Autore:
Ginsburg, A;
Indirizzi:
NHLBI, Sect Prot Chem, Biochem Lab, NIH, Bethesda, MD 20892 USA NHLBI Bethesda MD USA 20892 hem, Biochem Lab, NIH, Bethesda, MD 20892 USA
Titolo Testata:
JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY
fascicolo: 2, volume: 61, anno: 2000,
pagine: 425 - 436
SICI:
1388-6150(2000)61:2<425:RTIDUI>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACANTHAMOEBA MYOSIN-II; DODECAMERIC GLUTAMINE-SYNTHETASE; SUGAR PHOSPHOTRANSFERASE SYSTEM; ESCHERICHIA-COLI PHOSPHOENOLPYRUVATE; DIFFERENTIAL SCANNING CALORIMETRY; N-TERMINAL DOMAIN; STATISTICAL MECHANICAL DECONVOLUTION; SKELETAL-MUSCLE MYOSIN; AMINO-ACID-SEQUENCE; ENZYME-I;
Keywords:
Acanthamoeba myosin II rod coiled-coil; amino terminal domain of enzyme I of the phosphoenolpyruvate : sugar phosphotransferase system of E. coli; circular dichroism; differential scanning calorimetry; dodecameric glutamine synthetase; oligomeric protein domains; thermal unfolding; UV-spectra;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Ginsburg, A NHLBI, Sect Prot Chem, Biochem Lab, NIH, Bldg 3,Room 208, Bethesda, MD 20892 USA NHLBI Bldg 3,Room 208 Bethesda MD USA 20892 esda, MD 20892 USA
Citazione:
A. Ginsburg, "Reversible, thermally induced domain unfolding in oligomeric proteins - Spectral and DSC measurements", J THERM ANA, 61(2), 2000, pp. 425-436

Abstract

Spectral and differential scanning calorimetry (DSC) results for three oligomeric proteins are briefly reviewed. (A) Reversible, thermally-induced partial unfolding reactions in dodecameric glutamine synthetase from E. coli involve cooperative, two two-state transitions of subunits and demonstrate communication among subunits. (B) Thermal unfolding of intact Acanthamoeba myosin II is more cooperative than that of mammalian skeletal muscle myosin. Nucleotide-induced conformational changes thermally stabilize head domains in both myosins. The long dimeric coiled-coil rod of Acanthamoeba myosin II undergoes a reversible, cooperative, single two-state thermal transitionwith concomitant chain dissociation. (C) The amino terminal domain of enzyme I of the E. coli PEP:sugar phosphotransferase system is destabilized by phosphorylation of the active-site His 189.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 23:10:37