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
收藏
页码：51 / 58
页数：8
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