Influence of extrinsic factors on the conformational dynamics of industrially important proteins: A molecular perspective

Proteins are inherently dynamic molecules that require a stable structure to execute their biological functions. Variations in extrinsic factors such as temperature, pH, and solution conditions can induce structural changes in proteins that favor or negatively affect a protein’s functions. Interpreting the molecular basis of the structural changes of proteins would significantly accelerate the development of stable protein formulations for industrial applications. This thesis highlights the insights gained from the molecular dynamics simulations of two model proteins, which will further the understanding of the interplay between protein structure and dynamics.