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.

Electrophoresis of proteins across a transverse sodium dodecyl sulfate gradient / E. Gianazza, M. Vignati, O. Santi, G. Vecchio. - In: ELECTROPHORESIS. - ISSN 0173-0835. - 19:10(1998), pp. 1631-1641.

Electrophoresis of proteins across a transverse sodium dodecyl sulfate gradient

E. Gianazza
Primo
;
1998

Abstract

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.
Circular dichroism; Denaturant gradient gel electrophoresis; Proteins; Sodium dodecyl sulfate
Settore BIO/10 - Biochimica
1998
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/180958
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