Thermodynamic parameters of helix–coil transition in polypeptide chains. II. Poly‐L‐lysine
- 1 November 1971
- journal article
- Published by Wiley in Biopolymers
- Vol. 10 (11) , 2181-2197
- https://doi.org/10.1002/bip.360101112
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Thermodynamic parameters of helix‐coil transition in polypeptide chains I. Poly‐(L‐glutamic acid)Biopolymers, 1971
- Cooperativity of the helix-random coil transition determined from hydrodynamic dataBiopolymers, 1970
- Stability of the helical conformation of randomL-alanine-L-lysine copolymers in aqueous solutionBiopolymers, 1970
- Solution Properties of Synthetic Polypetides. VII. Approximate Expressions for Important Physical Quantities of Polypeptide MoleculesPolymer Journal, 1970
- Stability of the polyglutamic acid .alpha. helixJournal of the American Chemical Society, 1968
- Potentiometric titrations and the helix–coil transition of poly(L‐glutamic acid) and poly‐L‐lysine in aqueous salt solutionsBiopolymers, 1968
- The Conformational Transitions of Uncharged Poly-L-lysine. α Helix-Random Coil-β Structure*Biochemistry, 1967
- Experimental Free Energy and Enthalpy of Formation of the α Helix1The Journal of Physical Chemistry, 1966
- The Effects of Solvent Environment on the Optical Rotatory Dispersion Parameters of PolypeptidesBiophysical Journal, 1965
- The helix-coil transition in charged macromoleculesMolecular Physics, 1960