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Secondary structure prediction of scleractinia corals: a proteomic approach

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Title Secondary structure prediction of scleractinia corals: a proteomic approach
 
Creator Ramalingam, V
Rajaram, R
Suresh, V
 
Subject Scleractinians
Secondary structure
Protein function
 
Description 503-509
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.
 
Date 2013-09-02T12:21:32Z
2013-09-02T12:21:32Z
2013-08
 
Type Article
 
Identifier 0975-1033 (Online); 0379-5136 (Print)
http://hdl.handle.net/123456789/20910
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJMS Vol.42(4) [August 2013]