Kinetic analysis of the hydrodynamic transition accompanying protein folding using size exclusion chromatography. 1. Denaturant dependent baseline changes.
Size exclusion profiles of proteins with persistent conformations exhibit broad asymmetric peaks whose shape and elution times are dependent on denaturant concentration. The collective elution profiles were precisely simulated by an apparent binding model that treats the denaturant dependence in terms of an apparent matrix binding. The model requires three experimentally measurable parameters: the elution time for the unbound protein, an apparent association equilibrium constant for binding, and an apparent exchange time for binding. The denaturant dependence for each of these parameters is related to the accessible surface area of the protein.
Shalongo
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Department of Biochemistry, University of Iowa, Iowa City 52242.
Heid
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P
Stellwagen
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E
D000595:Amino Acid Sequence; D002850:Chromatography, Gel / Q000379:methods; D004798:Enzymes / Q000737:chemistry; D007700:Kinetics; D008433:Mathematics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D004798:Enzymes; D009842:Oligopeptides; D010455:Peptides; D011506:Proteins