Please use this identifier to cite or link to this item:
Title: Secondary structure prediction of scleractinia corals: a proteomic approach
Authors: Ramalingam, V
Rajaram, R
Suresh, V
Keywords: Scleractinians;Secondary structure;Protein function
Issue Date: Aug-2013
Publisher: NISCAIR-CSIR, India
Abstract: Frequency component analysis of the three corals viz. Acropora formosa (AF +70), Favia pallida (FP +70) and Montipora digitata (MD +70) indicated that the peptides were composed of Beta structure, comprising α-helix, β turn/sheet, extended strend and Random coil. Chemical property of the three sequences were calculated, the pI is 8.41 with molecular weight 35172.9 kDa, 8.24 with the molecular weight 42187.6 kDa and 9.25 with the molecular weight 36411.8 kDa. There are two domains were present in both AF +70 and FP +70, under the family of Cytochrome B N and Cytochrome B C. N-terminal refers to the start of a polypeptide terminated by an amino acid with free amine group. C-terminal refers to the end of the amino acid chain terminated by free carboxyl group. Transmembrane helix was predicted based on the positive and negative charged amino acids. Calcified organic matrix of scleractinian coral has a protein composition that is characterized by a predominance of aspartic acid. A binding study indicates that the organic matrix from the scleractinians has the ability to bind metal ions, cation and protein complex etc.
Page(s): 503-509
ISSN: 0975-1033 (Online); 0379-5136 (Print)
Appears in Collections:IJMS Vol.42(4) [August 2013]

Files in This Item:
File Description SizeFormat 
IJMS 42(4) 503-509.pdf215.53 kBAdobe PDFView/Open

Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.