In silico sequence analysis of predicted beta-amylase 7-like protein in Juglans regia L.
Abstract
Walnut (Juglans regia L.) is a deciduous tree of the Juglandaceae family. Beta-amylase (β-amylase, EC 3.2.1.2) is an enzyme that catalyses hydrolysis of glycosidic bonds in polysaccharides. In this study; sequence, physicochemical, and three-dimensional analyses of predicted β-amylase 7-like protein in Juglans regia using various bioinformatic tools were conducted. The physicochemical properties of the predict β-amylase 7-like protein were analyzed by using ExPASy ProtParam tool that revealed the molecular weight (MW), Isoelectric Points (pI), total number of negatively charged residues (Asp + Glu), total number of positively charged residues (Arg + Lys), instability index, aliphatic index, and GRAVY (Grand Average of Hydropathy) values. Subcellular localization using CELLO v.2.5, putative phosphorylation sites using NetPhos 3.1 server, domain analysis using Pfam, and secondary structure prediction using SOPMA were accom-plished. To predict the 3D structure of the predict β-amylase 7-like protein, homology models were applied using PSIPRED, RAMPAGE, and PyMOL programs. The results of our study provide insight into fundamental characteristics of the predicted β-amylase 7-like protein in Juglans regia.
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References
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