Electrophoretic characterization of the denatured states of staphylococcal nuclease.

doi:10.1006/jmbi.1994.1616

Back to search

Article

Electrophoretic characterization of the denatured states of staphylococcal nuclease.

Journal of molecular biology - 7 Oct 1994

Creighton T E, Shortle D

Abstract excerpt

The denatured state of staphylococcal (staph) nuclease has been shown to be altered by mutations, which complicates studies of stability of the folded state and may be important for the folding process. The relative hydrodynamic volumes as a function of urea concentration of staph nuclease, and o...

Topics

Calcium
Electrophoresis, Polyacrylamide Gel
Micrococcal Nuclease
Models, Chemical
Mutation
Protein Conformation
Protein Denaturation
Protein Folding
Thermodynamics
Thymine Nucleotides
Urea

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.