13C Nuclear magnetic resonance study of salt induced conformational change of basic polypeptides: Poly (L-lysine), poly (L-arginine), and poly (L-ornithine)-Reference-Cited by-同舟云学术

13C Nuclear magnetic resonance study of salt induced conformational change of basic polypeptides: Poly (L-lysine), poly (L-arginine), and poly (L-ornithine)

Published:1978-11 Issue:11 Volume:17 Page:2587-2599
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Saitô Hazime,Ohki Toyokazu,Kodama Masahiko,Nagata Chikayoshi

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference39 articles.

1. Helix-coil transition of poly-L-arginine: A comparison with other basic polypeptides

2. Helix formation of poly(L-lysine thiocyanate) in aqueous solutions

3. The solution conformation of poly(L-lysine). A Raman and infrared spectroscopic study

4. The effect of neutral salts on the conformational transition of poly-?-amino acids. I. Potentiometric titration and optical rotatory dispersion studies

5. Ion-binding and conformation of poly-L -methionine S -methylsulfonium salts in added salt systems

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3. Effect of neutral salts and methylglyoxal on the cis-trans equilibrium of n-methylacetamide. A 13-carbon nuclear magnetic resonance study;International Journal of Quantum Chemistry;2009-06-19

4. Synthesis and Conformational Transition of Surface-Tethered Polypeptide: Poly(l-lysine);Macromolecules;2003-08-01

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