Article
Staphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy.
Proceedings of the National Academy of Sciences of the United States of America - 18 Jan 1994
Jacobs M D, Fox R O
Abstract excerpt
Pulsed hydrogen-deuterium exchange during refolding was used to probe the protection of backbone amide hydrogens from solvent exchange of the staphylococcal nuclease Pro117-->Gly variant. The extent of exchange for 39 residues was determined by two-dimensional proton NMR after refolding for 5 ms...
Topics
- Amides
- Amino Acid Sequence
- Deuterium
- Genetic Variation
- Hydrogen
- Kinetics
- Magnetic Resonance Spectroscopy
- Micrococcal Nuclease
- Models, Molecular
- Molecular Sequence Data
- Molecular Structure
- Protein Folding
- Protein Structure, Secondary
