Conformational studies of alanine oligopeptides by nuclear magnetic resonance
- 1 May 1975
- journal article
- Published by Wiley in Biopolymers
- Vol. 14 (5), 901-914
- https://doi.org/10.1002/bip.1975.360140502
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Conformational Studies of Polymers and Copolymers of L-Aspartate Esters. III. Nuclear Magnetic Resonance SpectroscopyMacromolecules, 1971
- Conformational and kinetic studies of synthetic polypeptides by NMRBiopolymers, 1970
- On the controversy over “fast” and “slow” helix–coil transition rates in polypeptidesBiopolymers, 1970
- Optical Rotatory Dispersion and Nuclear Magnetic Resonance. Studies of Helix Coil Transitions in Poly-l-Arginine, Poly-l-Lysine and HistonesEuropean Journal of Biochemistry, 1970
- Orientation of Polypeptide Side Chains in SolutionNature, 1970
- Dynamics of the helix-coil transition in poly-L-ornithineJournal of the American Chemical Society, 1969
- Nuclear magnetic resonance investigation of the helix to random coil transformation in poly‐α‐amino acids. I. Poly‐L‐alanineBiopolymers, 1969
- Kinetic properties and the electric field effect of life helix–coil transition of poly(γ‐benzyl L‐glutamate) determined from dielectric relaxation measurementsBiopolymers, 1968
- Proton Magnetic Resonance and the Helix–Coil TransitionNature, 1968
- The dynamics of the helix‐coil transition in poly‐α, L‐glutamic acidBiopolymers, 1964