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Carbon-13 and Proton Nuclear Magnetic Resonance Observations of the Conformation of Poly(L-proline) in Aqueous Salt Solutions

✍ Scribed by Dorman, Douglas E.; Torchia, Dennis A.; Bovey, Frank A.

Book ID
121478041
Publisher
American Chemical Society
Year
1973
Tongue
English
Weight
320 KB
Volume
6
Category
Article
ISSN
0024-9297

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πŸ“œ SIMILAR VOLUMES

An infrared study on the conformation of
An infrared study on the conformation of poly-L-proline in concentrated aqueous salt solutions
✍ Charles A. Swenson πŸ“‚ Article πŸ“… 1971 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 341 KB πŸ‘ 2 views

The infrared absorption of poly-L-proline in concentrated aqueous salt solutions was measured in the fundanierital region. Of primary interest were the carbonyl absorption of the peptide linkage and the methylene C-H bending absorption of the pyrrolidine ring. These spectral regions each show an add

13C Nuclear magnetic resonance study of
13C Nuclear magnetic resonance study of salt induced conformational change of basic polypeptides: Poly (L-lysine), poly (L-arginine), and poly (L-ornithine)
✍ Hazime SaitΓ΄; Toyokazu Ohki; Masahiko Kodama; Chikayoshi Nagata πŸ“‚ Article πŸ“… 1978 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 553 KB

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.