Article
NMR studies of structure, hydrogen exchange, and main-chain dynamics in a disrupted-core mutant of thioredoxin.
Protein science : a publication of the Protein Society - 1 Dec 1996
De Lorimier R, Hellinga H W, Spicer L D
Abstract excerpt
Core-packing mutants of proteins often approach molten globule states, and hence may have attributes of folding intermediates. We have studied a core-packing mutant of thioredoxin, L78K, in which a leucine residue is substituted by lysine, using 15N heteronuclear two- and three-dimensional NMR. C...
Topics
- Escherichia coli
- Hydrogen
- Magnetic Resonance Spectroscopy
- Mutation
- Protein Folding
- Thioredoxins