Rath, L SJoshi, P NRaval, M KBiswal, U C1997-08-012009-05-271997-08-012009-05-271997-08-01Rath LS, Joshi PN, Raval MK, Biswal UC. Prediction of structure and organisation of chlorophyll a/b binding polypeptides in PS I and II. Indian Journal of Biochemistry & Biophysics. 1997 Aug; 34(4): 341-6http://imsear.searo.who.int/handle/123456789/26435Secondary structures, functionally important residues, antigenic sites, membrane spanning segments and hydropathicity of light harvesting chlorophyll a/b binding polypeptides (LHC) are predicted by theoretical methods from the amino acid sequence of the polypeptides. The reported structural features of the Pea LHC (Lhcb 1 gene product) from electron crystallographic studies have been compared by alignment with other types of chlorophyll a/b binding polypeptides for structural prediction. Fifteen conserved residues D85, D89, E113, H116, E/Q133, E/Q181, E189, D/N233, E252, N/H255, Q/E269, E/D/Q280, N281, H285, D288 (number indicates position in the aligned sequence), are identified which are potential ligands to Mg2+ of chlorophylls. Three amino acid residues D89, E/Q131 and D/N 233 are proposed as ligands to chlorophylls b2, a7 and b2 respectively, for which ligands are not identified in electron crystallographic study.engAmino Acid SequenceBinding SitesChlorophyll --metabolismLight-Harvesting Protein ComplexesMolecular Sequence DataPhotosynthetic Reaction Center Complex Proteins --chemistryProtein Structure, SecondarySequence Homology, Amino AcidJournal Article