A comparison between poly-α,l-ornithine and poly-α,l-lysine in solution: The effect of a CH2 group in the side chain on the conformation of poly-α-amino acids
- 1 February 1967
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 133 (2) , 206-218
- https://doi.org/10.1016/0005-2795(67)90060-8
Abstract
No abstract availableThis publication has 42 references indexed in Scilit:
- Van Der Waals Interaction and the Stability of Helical Polypeptide ChainsNature, 1965
- Influence of helix content and solvent environment on the optical rotatory dispersion parameters of polypeptidesJournal of Molecular Biology, 1963
- Sedimentation and diffusion of polyelectrolytes. Part II. Experimental studies with poly‐L‐lysine hydrohalidesBiopolymers, 1963
- Studies on the Binding of Ferriheme to Poly-L-lysine.Acta Chemica Scandinavica, 1963
- Contribution of Hydrophobic Interactions to the Stability of the Globular Conformation of ProteinsJournal of the American Chemical Society, 1962
- Conformational Aspects of Polypeptides. IV.1 Folded and Associated Forms of Oligomeric Peptides Derived from γ-Methyl GlutamateJournal of the American Chemical Society, 1962
- Effect of Polylysine on the Absorption Spectrum of HæminNature, 1961
- CONFORMATIONAL ASPECTS OF SYNTHETIC POLYPEPTIDES. II. CRITICAL RANGE FOR INTRAMOLECULAR HYDROGEN BONDINGJournal of the American Chemical Society, 1960
- Polypeptides. XVI. The Polydispersity and Configuration of Low Molecular Weight Poly-γ-benzyl-L-glutamates1Journal of the American Chemical Society, 1957
- Polypeptides. VIII. Molecular configurations of poly‐L‐glutamic acid in water‐dioxane solutionJournal of Polymer Science, 1957