Open AccessStructural Prediction andIn SilicoPhysicochemical Characterization for Mouse Caltrin I and Bovine Caltrin Proteins
Author(s) -
Ernesto Javier Grasso,
Adolfo Emiliano Sottile,
Carlos E. Coronel
Publication year - 2016
Publication title -
bioinformatics and biology insights
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 23
ISSN - 1177-9322
DOI - 10.4137/bbi.s38191
Subject(s) - in silico , threading (protein sequence) , homology modeling , calcium binding protein , computational biology , sequence homology , extracellular , biology , chemistry , bioinformatics , protein structure , biophysics , microbiology and biotechnology , calcium , biochemistry , peptide sequence , gene , enzyme , organic chemistry
It is known that caltrin (calcium transport inhibitor) protein binds to sperm cells during ejaculation and inhibits extracellular Ca 2+ uptake. Although the sequence and some biological features of mouse caltrin I and bovine caltrin are known, their physicochemical properties and tertiary structure are mainly unknown. We predicted the 3D structures of mouse caltrin I and bovine caltrin by molecular homology modeling and threading. Surface electrostatic potentials and electric fields were calculated using the Poisson-Boltzmann equation. Several different bioinformatics tools and available web servers were used to thoroughly analyze the physicochemical characteristics of both proteins, such as their Kyte and Doolittle hydropathy scores and helical wheel projections. The results presented in this work significantly aid further understanding of the molecular mechanisms of caltrin proteins modulating physiological processes associated with fertilization.
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