Electrophoresis of proteins across a transverse sodium dodecyl sulfate gradient.
We describe a new protocol for denaturant gradient gel electrophoresis, namely the migration of proteins across transverse sodium dodecyl sulfate (SDS)-gradients. We show how such gradients may be reproducibly cast, and demonstrate their stability with time once an appropriate SDS reservoir is arranged at the cathode. SDS affects both size and surface charge of the molecules, and influences the secondary and tertiary structure to a variable extent, even in opposite directions. Hence, distinct, sometimes complex, denaturation patterns may be observed for different proteins.
Istituto di Scienze Farmacologiche, Università di Milano, Italia. elisabetta.gianazza@unimi.it
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Gianazza
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Vignati
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Santi
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Vecchio
D002942:Circular Dichroism; D004586:Electrophoresis / Q000379:methods*; D007700:Kinetics; D009113:Muramidase / Q000032:analysis; D011489:Protein Denaturation; D011506:Proteins / Q000032:analysis*; D012967:Sodium Dodecyl Sulfate
D011506:Proteins; D012967:Sodium Dodecyl Sulfate; D009113:Muramidase