d-6-Deoxy-myo-inositol 1,3,4,5-tetrakisphosphate, a mimic of d-myo-inositol 1,3,4,5-tetrakisphosphate: biological activity and pH-dependent conformational properties

2004 ◽  
Vol 320 (4) ◽  
pp. 1262-1270 ◽  
Author(s):  
Graeme Horne ◽  
Clarisse Maechling ◽  
Andrea Fleig ◽  
Masato Hirata ◽  
Reinhold Penner ◽  
...  
Keyword(s):  
Biological Activity ◽  
Conformational Properties ◽  
Ph Dependent

Biological activity, pH dependent redox behavior and UV–Vis spectroscopic studies of naphthalene derivatives

2014 ◽  
Vol 140 ◽  
pp. 173-181 ◽  
Author(s):  
Abdur Rauf ◽  
Hanif Subhan ◽  
Rashda Abbasi ◽  
Bimalendu Adhikari ◽  
Aamir Hassan Shah ◽  
...  
Keyword(s):  
Biological Activity ◽  
Spectroscopic Studies ◽  
Redox Behavior ◽  
Naphthalene Derivatives ◽  
Ph Dependent

scholarly journals Dynamic behaviour of oxidized glutathione in solution investigated by nuclear magnetic resonance

1993 ◽  
Vol 71 (4) ◽  
pp. 506-511
Author(s):  
Claudio Rossi ◽  
Alessandro Donati ◽  
Sergio Ulgiati ◽  
Maria Rosaria Sansoni
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Biological Activity ◽  
Magnetic Resonance ◽  
Spin Label ◽  
Molecular Motion ◽  
Dynamic Behaviour ◽  
Oxidized Glutathione ◽  
Biological Functions ◽  
Conformational Properties ◽  
Structure In Solution

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 motion characterizes 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.

Conformational properties of the analgesic peptide dermorphin and their relationships to biological activity

1988 ◽  
Vol 164 (1-2) ◽  
pp. 153-164 ◽  
Author(s):  
Graziella Ranghino ◽  
Camillo Tosi ◽  
Luisa Barino ◽  
Raimondo Scordamaglia ◽  
Roberto Fusco
Keyword(s):  
Biological Activity ◽  
Conformational Properties ◽  
Analgesic Peptide
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