In view of the important biological functions of oxidized glutathione(GSSG), we investigated the correlation between dynamic and conformational properties and biological activity. Anisotropic molecular motioncharacterizes different GSSG molecular districts. This information, obtained by NMR carbon relaxation investigations, suggests that the peptide does not independently assume any stable structure in solution. Analysis of the effects of the addition of a stable spin label to the solution confirmed the absence of conformation of GSSG in D2O. Moreover, the paramagnetic effects observed on proton and carbon nuclei of oxidized glutathione suggest that the dipolar term is the main source of paramagnetic relaxation.
Dynamic behaviour of oxidized glutathione in solution investigated by Nuclear Magnetic Resonance
ULGIATI, Sergio;
1993-01-01
Abstract
In view of the important biological functions of oxidized glutathione(GSSG), we investigated the correlation between dynamic and conformational properties and biological activity. Anisotropic molecular motioncharacterizes different GSSG molecular districts. This information, obtained by NMR carbon relaxation investigations, suggests that the peptide does not independently assume any stable structure in solution. Analysis of the effects of the addition of a stable spin label to the solution confirmed the absence of conformation of GSSG in D2O. Moreover, the paramagnetic effects observed on proton and carbon nuclei of oxidized glutathione suggest that the dipolar term is the main source of paramagnetic relaxation.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
