Folding propensity and biological activity of peptides: New insights from conformational properties of a novel peptide derived fromVitreoscilla haemoglobin

Biopolymers ◽  
2007 ◽  
Vol 87 (1) ◽  
pp. 85-92 ◽  
Author(s):  
A. Bozzi ◽  
C. Coccia ◽  
A. Di Giulio ◽  
A. C. Rinaldi ◽  
A. Amadei ◽  
...  
Keyword(s):  
Biological Activity ◽  
Conformational Properties

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

A Study of the Conformational Properties of Glucagon in the Presence of Glycols

1974 ◽  
Vol 52 (6) ◽  
pp. 456-468 ◽  
Author(s):  
C. C. Contaxis ◽  
R. M. Epand
Keyword(s):  
Biological Activity ◽  
Tertiary Structure ◽  
Structural Response ◽  
Spectroscopic Properties ◽  
The Other ◽  
Monomeric Form ◽  
Conformational Properties ◽  
Α Helix

Elimination of the polymerization of glucagon has been achieved in the presence of glycols. The monomeric form of glucagon, found to be exclusively present under these conditions, is studied for its structural response to changes in the hydrophobicity of the environment. A reversible folding of the α-helix from about 0 to 80% is found to occur and it is suggested to proceed in two sequentially formed helical segments. Changes in the other spectroscopic properties are interpreted as changes in the tertiary structure. Implications for the biological activity are discussed.

ortho-Halogen naphthaleins as specific inhibitors of Lactobacillus casei thymidylate synthase. Conformational properties and biological activity

2003 ◽  
Vol 11 (6) ◽  
pp. 951-963 ◽  
Author(s):  
Stefano Ghelli ◽  
Marcella Rinaldi ◽  
Daniela Barlocco ◽  
Arianna Gelain ◽  
Piergiorgio Pecorari ◽  
...  
Keyword(s):  
Biological Activity ◽  
Thymidylate Synthase ◽  
Lactobacillus Casei ◽  
Conformational Properties ◽  
Specific Inhibitors
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