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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
Authors:Gian Paolo Lorenzi  Hans Juckle  Lera Tomasic  Carlo Pedone
Institution:Gian Paolo Lorenzi,Hans Jäuckle,Lera Tomasic,Carlo Pedone
Abstract: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 1H-nmr techniques. Right- and left-handed ↑↓β4.4-helices and left-handed β5.6-helices occur with the dodecapeptide. β4.4-Helices of opposite handedness occur also with the hexadecapeptide, but ↑↓β5.6-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 ↑↓β5.6-helices of D ,L -alternating oligovalines in chloroform solution.
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