Comparison of NH Exchange and Circular Dichroism as Techniques for Measuring the Parameters of the Helix−Coil Transition in Peptides†

Biochemistry ◽  
1997 ◽  
Vol 36 (28) ◽  
pp. 8435-8442 ◽  
Author(s):  
Carol A. Rohl ◽  
Robert L. Baldwin
Biopolymers ◽  
1979 ◽  
Vol 18 (2) ◽  
pp. 335-349 ◽  
Author(s):  
Shoichi Ikeda ◽  
Akira Fukutome ◽  
Toyoko Imae ◽  
Tomohiko Yoshida

1978 ◽  
Vol 56 (5) ◽  
pp. 622-627 ◽  
Author(s):  
Nga Ho-Duc ◽  
Hubert Daoust ◽  
Serge St-Pierre

The synthesis of the sequential polypeptides (N-δ-Z-L-Orn-γ-BzI-L-Glu)n and (N-δ-Z-L-Orn-β-BzI-L-Asp)n by solution methods is described. Both polypeptides are α helical in chloroform as shown by circular dichroism. However, the conformation in this solvent is rather fragile, since small additions of TFA to a dilute solution of the polypeptides in chloroform is sufficient to cause the helix-to-coil transition, as demonstrated by cd and nmr. It is postulated that the low stability of the helical conformation is attributed, in this case, to a cooperative collapse of the ordered conformation.


Author(s):  
John P. Robinson ◽  
J. David Puett

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.


1968 ◽  
Vol 65 ◽  
pp. 146-151 ◽  
Author(s):  
G. Scheibe ◽  
O. Wörz ◽  
F. Haimerl ◽  
W. Seiffert ◽  
J. Winkler

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