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Synthesis and conformational study of sequential polypeptides, (L-Ala-L-Val-Gly)n and (L-Val-L-Ala-Gly)n

✍ Scribed by Ryoichi Katakai; Masanao Oya; Yoshio Iwakura

Publisher
Wiley (John Wiley & Sons)
Year
1975
Tongue
English
Weight
590 KB
Volume
14
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

As an approach for elucidating the role of sequences of amino acids in protein structures, model polypeptides having the same composition but different sequences of amino acids, (L‐Ala‐L‐Val‐Gly)~n~ and (L‐Val‐L‐Ala‐Gly)~n~, have been prepared by the method involving facile monomer synthesis using N‐carboxy α‐amino acid anhydrides and N‐hydroxysuccinimide esters. The yields and the molecular weights of the polypeptides formed by polycondensation do not depend on the monomer concentrations, but on the sequences of the amino acids in the monomers. Infrared spectra in the solid state showed that (L‐Ala‐L‐Val‐Gly)~n~ can take the α‐helical conformation but (L‐Val‐L‐Ala‐Gly)~n~ cannot. The results suggest that the conformations of polypeptides are influenced by the sequences of the amino acids in the polypeptides.

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