Unravelling the effects of micro- and macroenvironments on protein dynamics: an in vitro study
Dr. Harekrushna Sahoo
Assistant Professor, Department of Chemistry, National Institute of Technology Rourkela, Odisha, India, Email: sahooh [at] nitrkl.ac.in - Homepage: www.sites.google.com/site/hsahoo
The structure and functions of proteins, a class of biomacromolecules responsible for various intracellular pathways and enzymatic processes, explicitly depend on the cellular environment (micro- and macro environments).1 Understanding of the biochemical processes involving proteins requires a comprehensive knowledge on the role of these environments in governing its folding and dynamics. Most of the in vitro assays dealing with the stability, conformations and functions of proteins are performed under conditions that are significantly different from the cellular environment. The physical phenomena of protein including stability, dynamics, and kinetics get affected due to the presence of various micro- and macromolecules as well as cell organelles.2 This difference restricts direct interpretations of in vivo mechanisms from the in vitro experimental findings.
In an attempt to understand and elucidate the precise functioning of proteins in a cellular environment, we have investigated the stability and dynamics of protein molecules under various physiologically relevant conditions. The role of microenvironment on cellular retinoic acid binding protein I (CRABP I) was studied using different salts whereas crowding agents like polyethylene glycol was employed to unravel the effects of macroenvironment. Along with, the impact of temporary components like dyes, drugs & co-solvent, which is because of accidental intake, also has been investigated using other proteins.3-5 Our findings demonstrate the significance of these biologically-active molecules on the protein stability and conformations along with functions and thus, provide a direct correlation of in vitro studies with the in vivo protein dynamics.
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