Stabilization of helix-turn-helix motif in short peptides. Rizvi, T., Petukhov, M., Tatsu, Y., & Yoshikawa, S. Journal of Chemical Society of Pakistan, 20(2):137-140, 1998. cited By 0![Stabilization of helix-turn-helix motif in short peptides [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper abstract bibtex Effective De novo designing of proteins is a great challenge and a critical test of our knowledge of protein structure. The main problem is the attainment of a protein with a defined fold for its specific function. This paper reports the synthesis and characterization of a series of helix - turn - helix (h-t-h) peptides with stable secondary and tertiary structures. In the order to optimize the stability of the anti-parallel coiled-coil structure of alpha helical hairpin peptides, all peplides with the same interacting helical regions but different number and sequences of residues in the turn region was examined. The turn region was incorporated between g and e2 of leucine zipper heptnd CD measurements showed that a four residue turn region was the best of stabilizing coiled coil structure in these peptides. The four residue turn sequence selected from h-t-h motifs of DNA binding proteins showed the highest helix stabilization in a short peptide of twenty nine amino acid residues.
@ARTICLE{Rizvi1998137,
author={Rizvi, T.Z. and Petukhov, M. and Tatsu, Y. and Yoshikawa, S.},
title={Stabilization of helix-turn-helix motif in short peptides},
journal={Journal of Chemical Society of Pakistan},
year={1998},
volume={20},
number={2},
pages={137-140},
note={cited By 0},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032334773&partnerID=40&md5=d5487d3a9ceae1a5682cd3b3f41a3240},
affiliation={Applied Chemistry Research Centre, PCSIR Laboratories Complex, Lahore, Pakistan; Biomolecular Engineering Laboratory, Department of Organic Materials, Osaka National Research Institute, Osaka, Japan},
abstract={Effective De novo designing of proteins is a great challenge and a critical test of our knowledge of protein structure. The main problem is the attainment of a protein with a defined fold for its specific function. This paper reports the synthesis and characterization of a series of helix - turn - helix (h-t-h) peptides with stable secondary and tertiary structures. In the order to optimize the stability of the anti-parallel coiled-coil structure of alpha helical hairpin peptides, all peplides with the same interacting helical regions but different number and sequences of residues in the turn region was examined. The turn region was incorporated between g and e2 of leucine zipper heptnd CD measurements showed that a four residue turn region was the best of stabilizing coiled coil structure in these peptides. The four residue turn sequence selected from h-t-h motifs of DNA binding proteins showed the highest helix stabilization in a short peptide of twenty nine amino acid residues.},
correspondence_address1={Rizvi, T.Z.; Applied Chemistry Research Centre, PCSIR Laboratories Complex, Lahore, Pakistan},
issn={02535106},
language={English},
abbrev_source_title={J. Chem. Soc. Pak.},
document_type={Article},
source={Scopus},
}
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