title: Electromechanical transduction: reduction-driven hydrophobic folding demonstrated in a model protein to perform mechanical work.
abstract: It has long been appreciated that hydrophobic folding is an important element of protein structure formation. Here it is demonstrated for the first time that the electrochemical or chemical reduction of a nicotinamide in a model protein, which increases hydrophobicity, can drive hydrophobic folding and assembly in such a way as to lift a weight or otherwise contract against a constant tensional force. The model protein, poly[0.73(GVGVP),0.27(GK(NMeN)GVP], can be gamma-irradiation cross-linked to form an elastic matrix which contracts on raising the temperature from below to above the transition range for hydrophobic folding and assembly. On reduction of the N-methyl nicotinamide, (NMeN), the transition temperature range is lowered from above to below 20 degrees C to drive contraction due to hydrophobic folding with the performance of mechanical work.
authors.affiliation: Laboratory of Molecular Biophysics, School of Medicine, University of Alabama at Birmingham 35294-0019.
authors.forename: D W
authors.initials: DW
authors.lastname: Urry
authors.forename: L C
authors.initials: LC
authors.lastname: Hayes
authors.forename: D C
authors.initials: DC
authors.lastname: Gowda
mesh_terms: D000595:Amino Acid Sequence; D003432:Cross-Linking Reagents; D004548:Elasticity; D004563:Electrochemistry / Q000379:methods; D007202:Indicators and Reagents; D007700:Kinetics; D008969:Molecular Sequence Data; D009536:Niacinamide; D010084:Oxidation-Reduction; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011506:Proteins / Q000138:chemical synthesis / Q000737:chemistry*; D013997:Time Factors
chemical_list: D003432:Cross-Linking Reagents; D007202:Indicators and Reagents; D010455:Peptides; D011506:Proteins; D009536:Niacinamide