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In silico analysis of adhesive foot proteins of mussels

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Title In silico analysis of adhesive foot proteins of mussels
 
Creator Singaravelu, Muthukumar
Ramalingam, Kirubagaran
Anishetty, Sharmila
 
Subject Adhesion
Foot proteins
Cement proteins
Dipeptide and Tripeptide patterns
 
Description 2175-2180
Byssal threads made up of foot proteins help the
mussels to colonize new habitats facilitating attachment in aqueous
environments. In the current study, we have analyzed mussel adhesive proteins,
foot protein 1 (fp1) and foot protein 3 (fp3) in terms of their amino acid
composition and dipeptide and tripeptide preferences. Further, analysis of
sequence around the post translationally modified fp1 shows a sequential
arrangement of decapeptide or octapeptide patterns. The pattern that was
derived from four species of Mytilus was
"Y-X(5)-Y-X(3)", while the three sequences from Perna virdis show "W-X(2)-W-X(6)" pattern and the four
sequences from Perna canaliculus show
octapeptide "Y-X(3)-Y-X(3)" pattern repeats. In silico analysis of amino acid composition using PERL program
confirms the significant role of amino acid residues. The dipeptide and
tripeptide analyses of cement proteins of barnacles and polychaetes were also
performed. Dipeptide and tripeptide analysis provided an overview of
compositional bias which is prevalent among marine invertebrate adhesive
protein complexes. The analyses of three groups of frequent macrofoulers
(mussels, barnacles and polychaetes) bring out the importance of individual
amino acids and dipeptides and tripeptides in underwater adhesion.
 
Date 2016-06-30T06:14:58Z
2016-06-30T06:14:58Z
2014-11
 
Type Article
 
Identifier 0975-1033 (Online); 0379-5136 (Print)
http://hdl.handle.net/123456789/34589
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJMS Vol.43(11) [November 2014]