The influence of glycerol on the structural properties of Fe(III)-horse heart myoglobin has been investigated by absorbance, CD and SR-SAXS spectroscopy. The results obtained indicate that both the tertiary and the secondary (alpha-helix) conformations of the protein are influenced by glycerol; in particular, an increase of approx. 8% in helical content was observed. Further, analysis of both the acid- and guanidine-induced denaturation transitions points to a glycerol-induced decreased stability of the tertiary structure; conversely, the alpha-helix conformation is found to be stabilized by the organic solvent. Finally, the SR-SAXS data show that gyration radius, cross-section and thickness of the protein increase in the presence of the organic solvent; however, the protein maintains a compact state.
Barteri, M., Gaudiano, M.c., Santucci, R. (1996). Influence of glycerol on the structure and stability of ferric horse heart myoglobin: A SAXS and circular dichroism study. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1295(1), 51-58 [10.1016/0167-4838(96)00010-6].
Influence of glycerol on the structure and stability of ferric horse heart myoglobin: A SAXS and circular dichroism study
SANTUCCI, ROBERTO
1996-01-01
Abstract
The influence of glycerol on the structural properties of Fe(III)-horse heart myoglobin has been investigated by absorbance, CD and SR-SAXS spectroscopy. The results obtained indicate that both the tertiary and the secondary (alpha-helix) conformations of the protein are influenced by glycerol; in particular, an increase of approx. 8% in helical content was observed. Further, analysis of both the acid- and guanidine-induced denaturation transitions points to a glycerol-induced decreased stability of the tertiary structure; conversely, the alpha-helix conformation is found to be stabilized by the organic solvent. Finally, the SR-SAXS data show that gyration radius, cross-section and thickness of the protein increase in the presence of the organic solvent; however, the protein maintains a compact state.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
