Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.

doi:10.1016/s0014-5793(98)00075-1

Back to search

Article

Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.

FEBS letters - 13 Feb 1998

Killick T R, Freund S M, Fersht A R

Abstract excerpt

The folding and unfolding of proteins is generally assumed to be so co-operative that the overall process may be followed by a single probe, such as tryptophan fluorescence. Folding kinetics of three mutants of barnase and chymotrypsin inhibitor 2 (CI2) were studied by real-time NMR. Rate constan...

Topics

Bacterial Proteins
Mutation
Nuclear Magnetic Resonance, Biomolecular
Peptides
Plant Proteins
Protein Folding
Ribonucleases
Time Factors

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.