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Titolo:
SOLVENT MODULATION OF THE STRUCTURAL HETEROGENEITY IN FEIII MYOGLOBINSAMPLES - A LOW-TEMPERATURE EPR INVESTIGATION
Autore:
BIZZARRI AR; CANNISTRARO S;
Indirizzi:
UNIV PERUGIA,DIPARTIMENTO FIS,CNR,UNITA INFM I-06100 PERUGIA ITALY UNIV PERUGIA,DIPARTIMENTO FIS,CNR,UNITA INFM I-06100 PERUGIA ITALY UNIV TUSCIA,DIPARTIMENTO SCI AMBIENTALI,SEZ CHIM & FIS I-01100 VITERBO ITALY
Titolo Testata:
European biophysics journal
fascicolo: 4, volume: 22, anno: 1993,
pagine: 259 - 267
SICI:
0175-7571(1993)22:4<259:SMOTSH>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTRON-PARAMAGNETIC-RES; PROTEIN DYNAMICS; HEME-PROTEINS; CONFORMATIONAL STATES; WATER; TRANSITION; RESONANCE; CRYSTALS; SPECTRA; DISTRIBUTIONS;
Keywords:
MYOGLOBIN; CONFORMATIONAL SUBSTATES; ELECTRON PARAMAGNETIC RESONANCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
A.R. Bizzarri e S. Cannistraro, "SOLVENT MODULATION OF THE STRUCTURAL HETEROGENEITY IN FEIII MYOGLOBINSAMPLES - A LOW-TEMPERATURE EPR INVESTIGATION", European biophysics journal, 22(4), 1993, pp. 259-267

Abstract

High spin FeIII myoglobin samples in solutions with different solventcomposition have been investigated at low temperature by Electron Paramagnetic Resonance spectroscopy. The g = 6 line of the spectrum has been analyzed in terms of a distribution of the two crystal field parameters DELTA1 and DELTA2. By means of the Angular Overlap Method, it has been shown that these distributions entail, in turn, a distribution in the iron-heme displacement along the normal to the heme-plane. The spread in this iron-heme distance, which can be connected with the binding action of the proximal histidine, has been proposed as a quantitative measurement of the structural heterogeneity (conformational substate landscape) displayed by the protein molecules. The results point out, moreover, that the solvent composition can affect the structural heterogeneity of the protein system. In particular, addition of glycerol, ethylene glycol and sucrose yields a significant reduction in the spread of the iron-heme displacement, while the presence of ammonium sulfate induces a change in the average position of the iron in the heme-plane. The role played by the solvent in the structure and dynamics of the protein, in connection also with the conformational substate distribution, is discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 22:20:12