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Titolo:
TEMPERATURE-DEPENDENCE OF THE G=6 EPR LINEWIDTH IN HIGH-SPIN FEIII MYOGLOBIN SAMPLES
Autore:
BIZZARRI AR; CANNISTRARO S;
Indirizzi:
UNIV PERUGIA,DIPARTIMENTO FIS,UNITA INFM CNR I-06100 PERUGIA ITALY UNIV PERUGIA,DIPARTIMENTO FIS,UNITA INFM CNR I-06100 PERUGIA ITALY UNIV TUSCIA,DIPARTIMENTO SCI AMBIENTALI,SEZ CHIM & FIS VITERBO ITALY
Titolo Testata:
Applied magnetic resonance
fascicolo: 4, volume: 6, anno: 1994,
pagine: 575 - 586
SICI:
0937-9347(1994)6:4<575:TOTGEL>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
PARAMAGNETIC-RES SPECTRA; HEME-PROTEINS; DYNAMICS; SOLVENT; WATER; HETEROGENEITY; SIMULATIONS; CONNECTION; RELAXATION; STRAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
A.R. Bizzarri e S. Cannistraro, "TEMPERATURE-DEPENDENCE OF THE G=6 EPR LINEWIDTH IN HIGH-SPIN FEIII MYOGLOBIN SAMPLES", Applied magnetic resonance, 6(4), 1994, pp. 575-586

Abstract

The temperature dependence of the g = 6 line of high spin FeIII aqueous mixed water-glycerol myoglobin samples has been investigated by EPRspectroscopy. The trend with the temperature of the linewidth has been analyzed by taking into account both a temperature-independent contribution from the frozen structural heterogeneity (conformational substate distribution) and the relaxation processes. The temperature-dependent line broadening process due to the spin-lattice relaxation has been singled out by simulation of the experimental data and put into relationship to the density of the vibrational states. The effect on the vibrational modes of the protein-solvent system, as induced by the addition of large amount of the glass-making solvent, glycerol, is discussed.

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Documento generato il 27/11/20 alle ore 23:39:41