Helix–coil transition of poly‐L‐arginine: A comparison with other basic polypeptides
- 1 November 1969
- journal article
- other
- Published by Wiley in Biopolymers
- Vol. 8 (5) , 685-688
- https://doi.org/10.1002/bip.1969.360080510
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
- The helix–coil transition of poly‐L‐lysine in methanol–water solvent mixturesBiopolymers, 1968
- Potentiometric titrations and the helix–coil transition of poly(L‐glutamic acid) and poly‐L‐lysine in aqueous salt solutionsBiopolymers, 1968
- Ion‐binding and conformation of poly‐L‐methionine S‐methylsulfonium salts in added salt systemsBiopolymers, 1968
- Helix-coil transition of poly-L-ornithine in solutionBiochemistry, 1968
- Helix formation of poly(L-lysine thiocyanate) in aqueous solutionsThe Journal of Physical Chemistry, 1967
- The Conformational Transitions of Uncharged Poly-L-lysine. α Helix-Random Coil-β Structure*Biochemistry, 1967
- 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 acidsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967
- Effect of Salts and Dioxane on the Coiled Conformation of Poly-L-glutamic Acid in Aqueous Solution*Biochemistry, 1965
- The Effect of Electrolytes on the Stability of the Deoxyribonucleate HelixJournal of the American Chemical Society, 1962
- Quantitative studies of the avidity of naturally occurring substances for trace metals. 2. Amino-acids having three ionizing groupsBiochemical Journal, 1952