Abstract
In the present work, the conformation of a model cytoplasmic protein, cellular retinoic acid-binding protein I (CRABP I), is investigated as a function of micro-environment in the terms of several anions, such as SO42−, HPO42−, and Cl− by employing fluorescence correlation spectroscopy (FCS) along with other biophysical techniques (fluorescence and circular dichroism (CD) spectroscopy). FCS observations revealed the impact of anions on the diffusion of protein as well as the hydrodynamic radius at room temperature. Fluorescence (steady-state and time-resolved lifetime) and CD results indicated the conformational change of the protein upon binding to different salts. Our results revealed the conformational changes of the protein during micro-environment conditions, which can be helpful to understand how cellular condition influences protein folding in vivo compared to in vitro folding.
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