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Nuclear magnetic resonance and optical spectroscopic studies of poly l and poly d alanine

✍ Scribed by E.M. Bradbury; H.W.E. Rattle

Book ID
103349983
Publisher
Elsevier Science
Year
1968
Tongue
English
Weight
992 KB
Volume
9
Category
Article
ISSN
0032-3861

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πŸ“œ SIMILAR VOLUMES

Proton magnetic resonance and optical sp
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The helix-coil transition has been studied by high-resolution NMR for three watersoluble polypeptides. Such systems are better models for protein behavior than those in TFA-CDC13 solvent. An upfield shift of ~7 cps is observed for the a-CH peak of poly(bg1utamic acid) and poly-clysine as the helix c

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ku, Tokyo, J a p a n 104 ## Synopsis A I3C-nmr study of the salt-induced helix-coil transition of the basic polypeptides poly(L-lysine) [(Lys),], poly(i-arginine) [(Arg),], and poly(i-ornithine) [(Orn),] was performed to serve as a reference of the helical portion of histones and other proteins.

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High-resolution nuclear magnetic resonance spectra at 100 MHz and 220 MHz have been obtained on two samples of poly-Galanine of Mering molecular weights (2500 and 42 500) in the chloroform-trifluoroacetic acid system under various conditions of solvent composition, temperature, and polypeptide conce