Influence of glycerol on the structure and stability of ferric horse heart myoglobin: A SAXS and circular dichroism study

被引：18

作者：

Barteri, M ^{[1
]}

Gaudiano, MC ^{[1
]}

Santucci, R ^{[1
]}

机构：

[1] UNIV ROMA TOR VERGATA,DIPARTIMENTO MED SPERIMENTALE & SCI BIOCHIM,I-00133 ROME,ITALY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1996年 / 1295卷 / 01期

关键词：

myoglobin; solvent effect; glycerol; conformational change; small-angle scattering X-ray analysis; circular dichroism; (horse heart);

D O I：

10.1016/0167-4838(96)00010-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：51 / 58

页数：8