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Titolo:
Some thermodynamic implications for the thermostability of proteins
Autore:
Rees, DC; Robertson, AD;
Indirizzi:
CALTECH, Howard Hughes Med Inst, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125 ard Hughes Med Inst, Pasadena, CA 91125 USA CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA CALTECH Pasadena CAUSA 91125 iv Chem & Chem Engn, Pasadena, CA 91125 USA Univ Iowa, Coll Med, Dept Biochem, Iowa City, IA 52242 USA Univ Iowa IowaCity IA USA 52242 d, Dept Biochem, Iowa City, IA 52242 USA
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 6, volume: 10, anno: 2001,
pagine: 1187 - 1194
SICI:
0961-8368(200106)10:6<1187:STIFTT>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
EGG-WHITE LYSOZYME; COLD-SHOCK PROTEIN; THERMOTOGA-MARITIMA; THERMAL-EXPANSION; STAPHYLOCOCCAL NUCLEASE; PRESSURE DENATURATION; RIBONUCLEASE-A; STABILITY; TEMPERATURE; DYNAMICS;
Keywords:
protein stability; thermal expansion; protein volumes; stability curve;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Rees, DC CALTECH, Howard Hughes Med Inst, 147-75CH, Pasadena, CA 91125 USACALTECH 147-75CH Pasadena CA USA 91125 CH, Pasadena, CA 91125 USA
Citazione:
D.C. Rees e A.D. Robertson, "Some thermodynamic implications for the thermostability of proteins", PROTEIN SCI, 10(6), 2001, pp. 1187-1194

Abstract

An analysis of the thermodynamics of protein stability reveals a general tendency for proteins that denature at higher temperatures to have greater free energies of maximal stability. To a reasonable approximation, the temperature of maximal stability for the set of globular, water-soluble proteinssurveyed by Robertson and Murphy occurs at T* similar to 283K, independentof the heat denaturation temperature, T-m. This observation indicates, at least for these proteins, that thermostability tends to be achieved throughelevation of the stability curve rather than by broadening or through a horizontal shift to higher temperatures. The relationship between the free energy of maximal stability and the temperature of heat denaturation is such that an increase in maximal stability of similar to0.008 kJ/mole/residue is, on average, associated with a 1 degreesC increase in T-m. An estimate of the energetic consequences of thermal expansion suggests that these effectsmay contribute significantly to the destabilization of the native state ofproteins with increasing temperature.

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Documento generato il 01/06/20 alle ore 01:25:27