Physiochemical and Functional Characterization of a Dominant Grain Endosperm Protein Called Glutelin in Rice (Oryza Sativa L.) Using in Silico Methods
glutelin protein, cupin family proteins, in silico, and homology modeling
Abstract
Glutelin protein is the most well-known abundant seed storage protein in rice seed endosperm. A total of 9 glutelin and glutelin type protein sequences from Oryza species available in uniport were evaluated by using bioinformatics tools to investigate physico-chemical properties, secondary structure prediction, putative phosphorylation sites and conserved motif search. Physicochemical analysis offers data such as pI, EC, Al, GRAVY and II about these sequences and the results showed that all glutelin protein sequences are basic, hydrophilic, thermo stable, having some extracellular portion. The secondary structure of the protein sequences were also predicted using SOPMA server. It was observed that alpha helix was predominant, followed by random coil, extended strand and least beta turn was found. Putative phosphorylation sites were also identified which are found to be conserved in plant species and the results showed that the most abundant phosphorylation site is serine residues in glutelin protein sequences.
Downloads
How to Cite
References
E Tecson, B Esmana, L Lontok, B Juliano (1971) Studies on the extraction and composition of rice endosperm glutelin and prolamin. 48, 186-181.
Ruth Villareal, Bienvenido Juliano (1978) Properties of glutelin from mature and developing rice grain. 17(2), 177-182.
C Mann (1997) Reseeding the green revolution. 277, 1038-1043.
A Brinegar, D Peterson (1982) Separation and characterization of oat globulin polypeptides. 219, 71-79.
Gregory Walburg, Brian Larkins (1983) Oat Seed Globulin. 72(1), 161-165.
E Derbyshire, D Wright, D Boulter (1976) Legumin and vicilin, storage proteins of legume seeds. 15, 3-24.
Eric Jain, Amos Bairoch, Severine Duvaud, Isabelle Phan, Nicole Redaschi, Baris Suzek, Maria Martin, Peter Mcgarvey, Elisabeth Gasteiger (2009) Infrastructure for the life sciences: design and implementation of the UniProt website. 10(1).
Elisabeth Gasteiger, Christine Hoogland, Alexandre Gattiker, S'everine Duvaud, Marc Wilkins, Ron Appel, Amos Bairoch (2005) Protein Identification and Analysis Tools on the ExPASy Server. 571-607.
C Geourjon, G Deléage (1995) SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. 11(6), 681-684.
N Blom, S Gammeltoft, S Brunak (1999) Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. 294(5), 1351-1362.
L Timothy, Charles Bailey, Elkan (1994) Fitting a mixture model by expectation maximization to discover motifs in biopolymers. 28-36.
Published
2017-01-25
Issue
Section
License
Copyright (c) 2016 Authors and Global Journals Private Limited
This work is licensed under a Creative Commons Attribution 4.0 International License.