Conformational studies of sequential polypeptides containing lysine and tyrosine | Zendy

St. Pierre S. | Zendy; Ingwall R. T. | Zendy; Verlander M. S. | Zendy; Goodman M. | Zendy

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Conformational studies of sequential polypeptides containing lysine and tyrosine

Author(s) -

St. Pierre S.,

Ingwall R. T.,

Verlander M. S.,

Goodman M.

Publication year - 1978

Publication title -

biopolymers

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.556

H-Index - 125

eISSN - 1097-0282

pISSN - 0006-3525

DOI - 10.1002/bip.1978.360170803

Subject(s) - lysine , chemistry , random coil , intramolecular force , tyrosine , stereochemistry , crystallography , circular dichroism , biochemistry , amino acid

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‐ L lysyl‐ L ‐lysine) and poly [ L ‐tyrosyl‐( L lysyl) 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.

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