Thermal stability of enzymes: influence of solvatation medium (a Raman spectroscopy study)

作者: D. Combes , I. Auzanneau , A. Zwick

DOI: 10.1016/B978-0-444-89372-7.50009-9

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摘要: Abstract Conformational studies of two enzymes (invertase and lysozyme), their interactions with solvent the effect alkali halides on conformational changes have been performed by means Raman spectroscopy. It has demonstrated that protective against thermal denaturation, exhibited studied salts can be correlated to a parameter (Δω) obtained from spectra in solution. From qualitative point view, higher is, more Δω decreases.

参考文章(4)
P. Terpstra, D. Combes, A. Zwick, Effect of salts on dynamics of water: A Raman spectroscopy study Journal of Chemical Physics. ,vol. 92, pp. 65- 70 ,(1990) , 10.1063/1.458418
I. Auzanneau, D. Combes, A. Zwick, Raman spectroscopic analysis of the effect of polyhydric alcohols on water Journal of Raman Spectroscopy. ,vol. 22, pp. 227- 231 ,(1991) , 10.1002/JRS.1250220406
Anthony V. Reddy, Robert MacColl, Frank Maley, Effect of oligosaccharides and chloride on the oligomeric structures of external, internal, and deglycosylated invertase. Biochemistry. ,vol. 29, pp. 2482- 2487 ,(1990) , 10.1021/BI00462A007
G Nemethy, W J Peer, H A Scheraga, EFFECT OF PROTEIN-SOLVENT INTERACTIONS ON PROTEIN CONFORMATION Annual Review of Biophysics and Bioengineering. ,vol. 10, pp. 459- 497 ,(1981) , 10.1146/ANNUREV.BB.10.060181.002331