## 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
Nuclear Magnetic Resonance Relaxation Study of Poly(γ-benzyl L-glutamate) Side-Chain Mobility in Helix-Coil Transition
✍ Scribed by Chien, Mingjien; Samulski, E. T.; Wade, Charles G.
- Book ID
- 125990730
- Publisher
- American Chemical Society
- Year
- 1973
- Tongue
- English
- Weight
- 629 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0024-9297
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The helix-coil transition temperature Tc of poly(Y-benzy1 bglutamate) in binary solvent mixtures of dichloroacetic acid and l,bdichlorobutane, 1-chlorooctane, or 1chlorododecane have been measured. A treatment is presented with which the transition enthalpy can be calculated from the observed depend
## Abstract The coil to helix conformational transitions undergone by poly‐γ‐benzyl‐~L~‐glutamate in solutions of haloacetic acids and various cosolvents were studied by means of proton magnetic resonance. The results indicate a very small solvent dependence of the α‐CH Helix–coil chemical shift di