Thermodynamic parameters from hydrogen exchange measurements.
Just as exchangeable hydrogens that are controlled by global unfolding can be used to measure thermodynamic parameters at a global level, hydrogens that are exposed to exchange by local unfolding reactions may be used to obtain locally resolved energy parameters. Results with the hemoglobin system demonstrate the ability of HX methods to locate functionally important changes in a protein and to measure the energetic contribution of each. These results offer the promise that HX measurements may be used to delineate, in terms of definable bonds and their energies and interactions, the network of interactions that Hb and other proteins use to produce their various functions.
Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia 19104, USA.
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Bai
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Englander
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Mayne
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Milne
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Englander
D002851:Chromatography, High Pressure Liquid; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology; D006454:Hemoglobins / Q000378:metabolism; D006859:Hydrogen / Q000378:metabolism*; D007700:Kinetics; D009711:Nucleotides / Q000378:metabolism; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011489:Protein Denaturation; D017510:Protein Folding; D013696:Temperature; D013816:Thermodynamics
D006146:Guanidines; D006454:Hemoglobins; D009711:Nucleotides; D010455:Peptides; D006859:Hydrogen; D019791:Guanidine