IMSc Webinar
Effects of charge mutations and phosphorylation on binding pocket dynamics in proteins
T S Sreevidya
IMSc, Chennai
PRE SYNOPSIS TALK:
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Proteins, intricate molecules composed of amino acids, play crucial roles in diverse biological processes. They form the structural foundation of cells and tissues, functioning as enzymes to accelerate vital chemical reactions and supporting cellular architecture. Additionally, proteins act as carriers, transporting essential elements throughout the body. The structure of a protein is fundamental to its interactions within the body, determining its function. Exploring the relationships among sequence, structure, and function has long captivated the molecular biology community. Key amino acid residues in proteins are investigated for their role in structure and function, providing insights for both understanding proteins and therapeutic purposes. Mutations can impact protein function by altering stability and modifying interactions with other biomolecules.
In particular, Post-translational modifications (PTMs) such as phosphorylation occur after protein synthesis, introducing new reactive groups and regulating cellular processes through reversible or irreversible mechanisms. In the thesis work, computational techniques including extensive molecular dynamics simulations, bioinformatics tools, docking are employed to investigate the effect of mutations of invariant charged residues and phosphorylation of key functional residues on the binding pocket dynamics and association with substrates. Wherever applicable, the computational results are compared with experimental results and in particular explain experimental outcomes on systems of interest.
We explore two protein systems:
1. Structural insights into the effects of mutations on charged binding pocket residues D124 and E131 on phosphopeptide binding to 14-3-3ζ Protein.
2. Regulatory role of tyrosine phosphorylation in PTP-PEST, investigated through bioinformatics and molecular dynamics simulations.
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