STABILIZATION OF HELIX-TURN-HELIX MOTIF IN SHORT PEPTIDES

Citation
Tz. Rizvi et al., STABILIZATION OF HELIX-TURN-HELIX MOTIF IN SHORT PEPTIDES, Journal of the Chemical Society of Pakistan, 20(2), 1998, pp. 137-140
Citations number
14
Categorie Soggetti
Chemistry
ISSN journal
02535106
Volume
20
Issue
2
Year of publication
1998
Pages
137 - 140
Database
ISI
SICI code
0253-5106(1998)20:2<137:SOHMIS>2.0.ZU;2-M
Abstract
Effective De novo designing of proteins is a great challenge and a cri tical test of our knowledge of protein structure. The main problem is the attainment of a protein with a defined fold for its specific funct ion. This paper reports the synthesis and characterization of a series of helix - turn - helix (h-t-h) peptides with stable secondary and te rtiary structures. In the order to optimize the stability of the anti- parallel coiled-coil structure of alpha helical hairpin peptides, all peptides with the same interacting helical regions but different numbe r and sequences of residues in the turn region was examined The turn r egion was incorporated between g and e(2) of leucine zipper heptad CD measurements showed that a four residue turn region was the best of st abilizing coiled coil structure in these peptides. The four residue tu rn sequence selected from h-t-h motifs of DNA binding proteins showed the highest helix stabilization in a short peptide of twenty nine amin o acid residues.