title: Protein folding, binding, and droplet formation in cell-like conditions.
abstract: The many bystander macromolecules in the crowded cellular environments present both steric repulsion and weak attraction to proteins undergoing folding or binding and hence impact the thermodynamic and kinetic properties of these processes. The weak but nonrandom binding with bystander macromolecules may facilitate subcellular localization and biological function. Weak binding also leads to the emergence of a protein-rich droplet phase, which has been implicated in regulating a variety of cellular functions. All these important problems can now be addressed by realistic modeling of intermolecular interactions. Configurational sampling of concentrated protein solutions is an ongoing challenge.
authors: Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.
authors: Sanbo
authors: S
authors: Qin
authors: Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA. Electronic address: hzhou4@fsu.edu.
authors: Huan-Xiang
authors: HX
authors: Zhou
mesh_terms: D002477:Cells / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D011506:Proteins