Journal
JOURNAL OF THEORETICAL BIOLOGY
Volume 283, Issue 1, Pages 92-102Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jtbi.2011.05.014
Keywords
Helix interactions; Heptad motif; Side-chain packing; Protein conformation; Glutathione S-transferase
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Helix-helix parallel interfaces can be characterized by certain combinations of amino acids, which repeatedly occur at core positions a and d (leucine zipper nomenclature) in homologous and nonhomologous proteins and influence interhelical angles. Applied for the prediction of interhelical angles in glutathione S-transferase, intracellular chloride channel and annexin molecules from various sources, correct results were achieved in 58 out of 62 proteins. Interhelical angles are found to correlate with the conformation of the glutathione S-transferase ligands glutathione, s-hexylglutathione, glutathione sulfonic acid, and glutathione-s-dinitrobenzene. (C) 2011 Elsevier Ltd. All rights reserved.
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