Temperature-dependent β structure-random coil conversion of poly(S-carboxymethyl-l-cysteine)
Author:
Publisher
Elsevier BV
Subject
Polymers and Plastics,Materials Chemistry,Organic Chemistry
Reference31 articles.
1. The Conformational Transitions of Uncharged Poly-L-lysine. α Helix-Random Coil-β Structure*
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4. Kinetics and thermodynamics of the α helix ⇄ β transconformation of poly(L-lysine) and L-leucine copolymers. Compensation phenomenon
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Monte Carlo Simulation of the β-sheet-Random Coil Transition of a Homopolypeptide: II. Kinetics;Japanese Journal of Applied Physics;1998-06-15
2. The β Sheet ⇌ Coil Transition of Polypeptides, as Determined by Circular Dichroism;Circular Dichroism and the Conformational Analysis of Biomolecules;1996
3. Correlation between the rate of chain folding and the stability of the .beta.-structure of a polypeptide;The Journal of Physical Chemistry;1990-05
4. Kinetics of pH-induced random coil-.beta.-structure conversion of poly[S-(carboxymethyl)-L-cysteine];Macromolecules;1989-02
5. Chain length dependence of solubility of monodisperse polypeptides in aqueous solutions and the stability of the .beta.-structure;The Journal of Physical Chemistry;1988-10
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