Denatured state structural property determines protein stabilization by macromolecular crowding: a thermodynamic and structural approach.

ABSTRACT: Understanding of protein structure and stability gained to date has been acquired through investigations made under dilute conditions where total macromolecular concentration never surpasses 10 g l(-1). However, biological macromolecules are known to evolve and function under crowded intracellular environments that comprises of proteins, nucleic acids, ribosomes and carbohydrates etc. Crowded environment is known to result in altered biological properties including thermodynamic, structural and functional aspect of macromolecules as compared to the macromolecules present in our commonly used experimental dilute buffers (for example, Tris HCl or phosphate buffer). In this study, we have investigated the thermodynamic and structural consequences of synthetic crowding agent (Ficoll 70) on thr

SUBMITTER: Mittal S 

PROVIDER: S-EPMC3827121 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature