Protein denaturant binding polynomials.
We show how moments of the denaturant binding distribution function can be extracted from experimental data on the denaturation of a protein as a function of the concentration of denaturant and how in turn these moments can be used to construct the denaturant binding distribution function. This approach is similar to our recent work on using the maximum-entropy method to construct ligand-binding distributions from moments obtained from titration curves for nucleic acids and proteins. As an example we take literature data on the denaturation of ferro- and ferricytochrome c by guanidine hydrochloride and from it construct the denaturant binding polynomial and binding distribution function for the unfolded protein.
Poland
Douglas
D
Department of Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218, USA. poland@jhu.edu
D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism; D016208:Databases, Factual; D019277:Entropy; D019791:Guanidine / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D008956:Models, Chemical; D016011:Normal Distribution; D011485:Protein Binding; D011489:Protein Denaturation; D017186:Titrimetry
D003574:Cytochrome c Group; D008024:Ligands; D019791:Guanidine