Can I read Solution structure of peptides containing two dehydro-phenylalanine residues: A CD investigation on EtoBox?

Solution structure of peptides containing two dehydro-phenylalanine residues: A CD investigation by Osvaldo Pieroni; Adriano Fissi; Claudio Pratesi; Pier Andrea Temussi; Francesco Ciardelli is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Solution structure of peptides containing two dehydro-phenylalanine residues: A CD investigation about?

4 ) , containing two dehydro-phenylalanine ( APhe ) residues, were synthesized and the solution structure investigated in various solvents. The nmr and CD measurements indicate that all the dehydropeptides examined adopt 310-helical conformations in solution. The tripeptides 1 and 2 exibited an intense negative CD exciton couplet, which was assigned to the right-handed screw sense, while the tetrapeptide 3 displayed a CD couplet having opposite sign, which was assigned to the left-handed helical sense. In the pentapeptide 4 the sense of the helix was found to vary with solvent and temperature, as demonstrated by the sign reversal of the CD spectrum. The right-handed sense dominates in hexafluoro-2-propanol, whereas a left-handed helix prevails in chloroform, acetonitrile and methanol. A crucial role for this behavior is likely to be played by the two alanine residues positioned respectively at the head and tail of the sequence, which favor conformations having opposite screw senses.

Who reads Solution structure of peptides containing two dehydro-phenylalanine residues: A CD investigation?

Author

Osvaldo Pieroni; Adriano Fissi; Claudio Pratesi; Pier Andrea Temussi; Francesco Ciardelli

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

1993

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)