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Influence of the peptide chain length on the stability of double‐stranded β‐helical species of D , L ‐alternating oligovalines in chloroform solution
Author(s) -
Lorenzi Gian Paolo,
Jäuckle Hans,
Tomasic Lera,
Pedone Carlo
Publication year - 1983
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.360220125
Subject(s) - chemistry , chloroform , oligomer , helix (gastropod) , peptide , crystallography , chain (unit) , stereochemistry , double stranded , distribution (mathematics) , biochemistry , dna , polymer chemistry , chromatography , physics , ecology , astronomy , snail , biology , mathematical analysis , mathematics
The type and distribution of the β‐helixes occurring in chloroform solutions of Boc‐(L‐Val‐D‐Val) 6 ‐OMe and Boc‐(L‐Val‐D‐Val) 8 ‐OMe have been studied by using 1 H‐nmr techniques. Right‐ and left‐handed ↑↓β 4.4 ‐helices and left‐handed β 5.6 ‐helices occur with the dodecapeptide. β 4.4 ‐Helices of opposite handedness occur also with the hexadecapeptide, but ↑↓β 5.6 ‐helices could not be detected with this oligomer. At equilibrium, at 25°C, the double helix of the dodecapeptide is only moderately populated. These results indicate that increasing the chain length has a destabilizing effect on the ↑↓β 5.6 ‐helices of D , L ‐alternating oligovalines in chloroform solution.