Quantitative measurement of the solvent accessibility of histidine imidazole groups in proteins.

ABSTRACT: We report a method for expressing the solvent accessibility of histidine imidazole groups in proteins. The method is based on measuring the rate of the hydrogen exchange (HX) reaction of the imidazole C(ε1)-hydrogen. The rate profile of the HX reaction as a function of pH gives a sigmoidal curve, which reaches the maximal rate constant (k(max)) on the alkaline side of the sigmoidal curve. To quantitatively describe the solvent accessibility of imidazole groups in proteins, it is necessary to compare the k(max) of the imidazole groups with their intrinsic k(max) ((i)k(max)), the maximal rate constants for the given imidazole groups when they are fully exposed to the bulk solvent. However, the mechanism of the HX reaction suggests that the (i)k(max) of an imidazole group differs depending on

SUBMITTER: Mullangi V 

PROVIDER: S-EPMC3462353 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature