Optical Rotatory Dispersion and Nuclear Magnetic Resonance : Studies of Helix → Coil Transitions in Poly-l-Arginine, Poly-l-Lysine and Histones
✍ Scribed by M. Boublík; E. M. Bradbury; C. Crane-Robinson; H. W. E. Rattle
- Book ID
- 115112246
- Publisher
- John Wiley and Sons
- Year
- 1970
- Tongue
- English
- Weight
- 531 KB
- Volume
- 12
- Category
- Article
- ISSN
- 1432-1327
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📜 SIMILAR VOLUMES
## Abstract There have been many reports that the nuclear magnetic resonance (nmr) spectra of a large number of polypeptides exhibit peak doubling of the α‐carbon and the α‐carbon proton in the helix–coil transition region. One apparent exception to this generalization has been polypeptides with io
Water-insoluble films of poly-L-lysine, crosslinked with formaldehyde, were suspended in aqueous media and their relative lengths measured as a function of pH. A sharp transition of the polymer was observed in the pH range which corresponded with that observed in polylysine solutions by optical rota
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.