How osmolytes influence hydrophobic polymer conformations: A unified view from experiment and theory
Copyright policy )How osmolytes influence hydrophobic polymer conformations: A unified view from experiment and theory
SignificanceOsmolytes influence protein structure by either promoting (protecting osmolytes) or disrupting (denaturing osmolytes) the folding process. Current consensus is that protecting osmolytes [trimethylamine N-oxide (TMAO)] act by being excluded from the protein surface while denaturing osmolytes (urea) bind to it. However there is little knowledge about the molecular mechanism of osmolyte action on hydrophobic macromolecules, which form the core of most proteins. This work, through a combination of single-molecule atomic force microscopy experiments and computer simulations, investigates the collapse behavior of a hydrophobic polymer polystyrene in TMAO and urea. The mechanism of osmolyte action on hydrophobic macromolecules is distinct from that of a protein, but, despite key differences, both mechanisms comply with the standard thermodynamic theory of preferential osmolyte binding.
- Sorbonne University France
- University of Toronto Canada
- PSL Research University France
- TIFR Centre for Interdisciplinary Sciences India
- Laboratory of Theoretical Biochemistry France
Protein Folding, Polymers, Protein Conformation, Normal Distribution, [SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, Molecular Dynamics Simulation, Stress, Microscopy, Atomic Force, Urea: chemistry, Polystyrenes: chemistry, Methylamines, Urea, Computer Simulation, Proteins: chemistry, Microscopy, Polymers: chemistry, Atomic Force, Proteins, Water, Water: chemistry, Mechanical, Methylamines: chemistry, Solvents: chemistry, Solvents, Polystyrenes, Thermodynamics, Stress, Mechanical, Hydrophobic and Hydrophilic Interactions, Software, Protein Binding
Protein Folding, Polymers, Protein Conformation, Normal Distribution, [SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, Molecular Dynamics Simulation, Stress, Microscopy, Atomic Force, Urea: chemistry, Polystyrenes: chemistry, Methylamines, Urea, Computer Simulation, Proteins: chemistry, Microscopy, Polymers: chemistry, Atomic Force, Proteins, Water, Water: chemistry, Mechanical, Methylamines: chemistry, Solvents: chemistry, Solvents, Polystyrenes, Thermodynamics, Stress, Mechanical, Hydrophobic and Hydrophilic Interactions, Software, Protein Binding
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