Unit 6 Protein Interactions

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Discussion Assignment Unit Six Protein interactions involve the contacts between two or more protein molecules, protein-nucleic acid, protein-ligand, or protein-membrane—which are crucial for various cellular processes like protein synthesis and degradation, signal transduction, metabolic pathways, immune responses, enzyme activity regulation, and so on. These protein interactions are determined by the protein structure and kinetics. Interactions will induce a conformational change in the protein and/or the associated molecule.

My favorite protein is chaperone—a helping protein that assists proteins in achieving proper folding, stability, and function. Several interplay of mechanisms that facilitates protein-protein interactions, folding and …show more content…
Their hydrophobic core binds to the exposed hydrophobic regions of unfolded proteins (Kawagoe, Ishimori, & Saio, 2022b). Then chaperones undergo conformational changes when they bind to client proteins, which allows them to encapsulate and protect the client proteins (Kawagoe, Ishimori, & Saio, 2022b).

Functional Kinetics Chaperones may act as holdases, foldases or disaggregases based on the specific function. They act as holdases by binding to client proteins and preventing misfolding, and aggregation (Kawagoe, Ishimori, & Saio, 2022). They can also act as foldases by catalysing the folding of client proteins to their native states (Kawagoe, Ishimori, & Saio, 2022). While, they may act as disaggregates by breaking down protein aggregates and fibrils. Chaperones can also act on other chaperones or co-chaperones to form complexes.

Chaperone client protein interactions involve rapid binding and release kinetics—transient and dynamic in nature. Chaperones kinetic mechanisms involve induced-fit mechanisms, where it binds with a client protein and induces conformational changes in chaperone; allosteric regulation can also occur where the binding of one protein affects that of
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