NMR-Monitored Hydrogen Exchange Study on the Conformational Stability of RNase A: The effect of cationic gemini surfactants (original) (raw)

2013

Abstract

Because of the many applications of surfactants in bioscience, drug delivery, and biotechnological processes, they are one of the most significant classes of applied ligands and their interaction with different proteins has been studied widely. The conformational stability of ribonuclease A (RNase A) has been measured at the per residue level by NMR-monitored hydrogen exchange in the absence and presence of cationic gemini surfactants. The hydrogen/deutrium exchange mechanism of RNase A has been found EXII in these conditions. We used gemini surfactants alkanediyl -α,ω-bis (Hydroxy ethyl methyl hexadecyl ammonium bromide) in this study. 1D NMR experiments showed gemini surfactants bind to DSS. 2D 1H-NMR spectroscopy shows that the conformation of RNase A is unaffected at acidic pH where this protein is positively charged, although hydrogen exchange results shows that the conformational stability of RNase A is slightly lowered at high molar ratios and acidic pH. At low molar ratios, ...

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