title: Nonadditive effects of mixed crowding on protein stability.
abstract: The crowded environments inside cells can have significant effects on the folding stability and other biophysical properties of proteins. In this study on how macromolecular crowding affects protein folding, we took a significant step toward realistically mimicking intracellular environments by using a mixture of two crowding agents, Ficoll and dextran. We found that the mixed crowding exerts a greater stabilizing effect than the sum of the two individual crowding agents. Therefore, the composition of crowders, not just the total concentration, has a significant influence on the effects of crowding on protein folding. Since the composition of intracellular macromolecules varies within the lifetime of a cell, our finding may provide an explanation for age being an important risk factor for protein aggregation-related diseases such as Alzheimer's disease and Parkinson's disease.
authors.affiliation: Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA.
authors.forename: Jyotica
authors.initials: J
authors.lastname: Batra
authors.forename: Ke
authors.initials: K
authors.lastname: Xu
authors.forename: Huan-Xiang
authors.initials: HX
authors.lastname: Zhou
mesh_terms: D003911:Dextrans / Q000737:chemistry; D005362:Ficoll / Q000737:chemistry; D008954:Models, Biological; D017510:Protein Folding; D055550:Protein Stability; D022021:Tacrolimus Binding Proteins / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D003911:Dextrans; D005362:Ficoll; D022021:Tacrolimus Binding Proteins