Barteri M, Gaudiano M C, Santucci R
Dipartimento di Chimica, Universitá degli Studi di Roma La Sapienza, Italy.
Biochim Biophys Acta. 1996 Jun 7;1295(1):51-8. doi: 10.1016/0167-4838(96)00010-6.
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.
通过吸光度、圆二色光谱（CD）和小角X射线散射光谱（SR-SAXS）研究了甘油对Fe(III)-马心肌红蛋白结构性质的影响。所得结果表明，甘油会影响蛋白质的三级结构和二级结构（α-螺旋）；特别是，观察到螺旋含量增加了约8%。此外，对酸诱导和胍诱导的变性转变的分析表明，甘油会导致三级结构稳定性降低；相反，发现α-螺旋构象被有机溶剂稳定。最后，SR-SAXS数据表明，在有机溶剂存在下，蛋白质的回转半径、横截面和厚度会增加；然而，蛋白质保持紧密状态。
