This method is representative of various cross-linking reactions and is one of the oldest and most practical. It allows the formation of intermolecular bridges between proteins and the linking of different proteins. It is also an effective tool for studying the interactions between protein subunits. The degree of cross-linking depends on the distance between the reacting groups and the reaction rate. By controlling the cross-linking reaction time, it is possible to study the steps of protein polymerization, obtain spatial structure information, and also obtain many homologous binders with different chain lengths, which can be used to study the relationship between cross-linking and distance between protein subunits. Source: Laboratory Manual of Enzymology

Operation method

basic program

Materials and Instruments

Protein Dimethylimine
Triethanolamine hydrochloride Neutral buffer

Move

The "reagents" required for the experiment are specified in "Others".

Mixed dimethylimine solution at a final concentration of 1-12 mg/ml and protein dissolved in 0.2 mol/L triethanolamine hydrochloride at pH 8.5 at a concentration of 0.4-5 mg/ml for 3 h at room temperature. Dialyze with neutral buffer.

Common Problems

Reagents:

0.2 mol/L triethanolamine hydrochloride, pH 8.5

Dimethylimine (dihydrochloride, Mr = 273.2, solution prepared with 0.2 mol/L triethanolamine hydrochloride, pH 8.5, ready to use, e.g., 3 mg/ml)

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