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Conformational studies of sequential polypeptides containing lysine and tyrosine

✍ Scribed by S. St. Pierre; R. T. Ingwall; M. S. Verlander; M. Goodman


Publisher
Wiley (John Wiley & Sons)
Year
1978
Tongue
English
Weight
635 KB
Volume
17
Category
Article
ISSN
0006-3525

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✦ Synopsis


Abstract

The conformation of three sequential copolypeptides, poly(L‐tyrosyl‐L‐lysine), poly(L‐tyrosyl‐L‐lysyl‐L‐lysine), and poly[L‐tyrosyl‐(L‐lysyl)~2~‐L‐lysine] have been studied by a variety of techniques, including CD, ir spectroscopy, analytical ultracentrifugation, and x‐ray diffraction. Depending upon the pH and sovent composition, poly(L‐tyrosyl‐Llysyl‐L‐lysine) and poly [L‐tyrosyl‐(Llysyl)~2~‐L‐lysine] can adopt either the α‐helical or random‐coil conformation, while poly(L‐tyrosyl‐L‐lysine) forms either inter‐ or intramolecular β‐structures.


📜 SIMILAR VOLUMES


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## Abstract The α‐helix–coil transition of poly‐L‐leucine, poly‐L‐alanine and poly‐L‐methionine in chloroform–trifluoroacetic acid system was studied by nuclear magnetic resonance (NMR) and optical rotatory dispersion (ORD). The kinetics of the hydrogen–deuterium exchange in the peptide was also fo