Premium
Observation of orientation and relaxation of protein‐sodium dodecyl sulfate complexes during pulsed intermittent field polyacrylamide gel electrophoresis
Author(s) -
Brassard Éric,
Turmel Chantal,
Noolandi Jaan
Publication year - 1991
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150120509
Subject(s) - sodium dodecyl sulfate , polyacrylamide gel electrophoresis , chemistry , gel electrophoresis , gel electrophoresis of proteins , chromatography , polyacrylamide , electrophoresis , sodium , relaxation (psychology) , molecular mass , pulsed field gel electrophoresis , biophysics , biochemistry , biology , polymer chemistry , organic chemistry , neuroscience , gene , genotype , enzyme
Polyacrylamide gel electrophoresis (PAGE) of proteins denatured with SDS (sodium dodecyl sulfate) has been used successfully to separate proteins according to their molecular mass. In spite of the extensive use of this technique, the motion of the protein‐SDS complex in a polyacrylamide gel is still not understood. Here we report on the observation of the orientation (in the field direction) and relaxation of protein‐SDS complexes during pulsed intermittent field PAGE experiments. The results give an indication of the stiffness of the molecules and may be useful for the development of a technique to improve the separation of large proteins using pulsed electric fields.