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Histidine hydrogen exchange protein folding

Histidine Hydrogen Exchange for Analysis of Protein Folding, Structure, and Function... [Pg.165]

In Equations 10.10 and 10.11, is the observed histidine hydrogen exchange rate. Equation 10.10 holds for folded proteins in which the histidine hydrogen exchange reaction requires the global... [Pg.176]

The chemical denaturant-dependent histidine hydrogen exchange protocol was initially developed and applied to several model protein systems including RNase A, myoglobin, and bovine carbonic anhydrase (BCA) II [32]. RNase A and myoglobin are known to have two-state folding behavior. BCA II is a non-two-state folding protein that is known to have a partially folded... [Pg.177]

In Equation 10.8, AG is the folding free energy of the protein, is the first-order rate constant of the slow hydrogen exchange reaction at the C-2 position in the imidazole side chain of an unprotected histidine, m is 54G, / 5[denaturant], T is the temperature in Kelvin, R is the ideal gas constant, and [P] is the protein concentration expressed in n-ma- equivalents. Equation 10.8 can be daived from Equation 10.9, which is commonly used in the linear extrapolation method (LEM) to analyze denaturant-induced equilibrium unfolding curves [34] ... [Pg.176]


See other pages where Histidine hydrogen exchange protein folding is mentioned: [Pg.165]    [Pg.175]    [Pg.175]    [Pg.177]    [Pg.177]    [Pg.179]    [Pg.180]    [Pg.180]    [Pg.181]    [Pg.182]    [Pg.179]    [Pg.286]   
See also in sourсe #XX -- [ Pg.177 , Pg.178 , Pg.179 ]




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