Chain condensation in protein folding.
Three reactions (relaxation times: tau 1 = 140 +/- 8 ms, tau 2 = 840 +/- 30 ms and tau 3 = 30 + 3 s, at pH 7.0 at 25 degrees C) have been resolved by the stopped-flow kinetic method for the folding of the acid denatured staphylococcal nuclease (Chen et al (1991) J Mol Biol 220, 771; Biochemistry (1992) 31, 1483). Of the three reactions only the tau 2 reaction was dependent on the viscosity of the solution in a manner consistent with the diffusion/collision/coalescence model. Experiments with site-directed mutagenesis suggest that the forming of local structures by the electrostatic interactions between Glu75 and His121 and Lys9 may induce the chain condensation.
Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon.
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D004058:Diffusion; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008836:Micrococcal Nuclease / Q000737:chemistry*; D017510:Protein Folding; D014783:Viscosity
D008836:Micrococcal Nuclease