Nature of amino acid side chain and ?-helix stability
- 1 July 1975
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 14 (7) , 1381-1393
- https://doi.org/10.1002/bip.1975.360140706
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Synthesis and conformational studies of model histones. Sequential and random polypeptides with the composition L-lysyl-L-alanyl-glycineBiochemistry, 1974
- Influence of isopropanol‐water solvent mixtures on the conformation of poly‐L‐lysineBiopolymers, 1973
- Contribution of the free energy of mixing of hydrophobic side chains to the stability of the tertiary structure of proteinsJournal of Theoretical Biology, 1973
- The effect of tert‐butanol on the conformational stability of poly‐L‐glutamic acid: The role of side‐chain interactionsBiopolymers, 1973
- Thermodynamic parameters of helix–coil transition in polypeptide chains. II. Poly‐L‐lysineBiopolymers, 1971
- Solution properties of synthetic polypeptides. VI. Helix-coil transition of poly-N5-(3-hydroxypropyl)-L-glutamineBiopolymers, 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
- New chain conformations of poly(glutamic acid) and polylysineBiopolymers, 1968
- Conformational Analysis of Macromolecules. IV. Helical Structures of Poly-L-Alanine, Poly-L-Valine, Poly-β-Methyl-L-Aspartate, Poly-γ-Methyl-L-Glutamate, and Poly-L-TyrosineThe Journal of Chemical Physics, 1967
- Stable Conformations of Polyamino Acid Helices1Journal of the American Chemical Society, 1966