Article
Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink.
Folding & design - 1 Jan 1996
Barbar E, Barany G, Woodward C
Abstract excerpt
BACKGROUND: NMR studies of denatured states, both fully unfolded and partially folded, give insight into the conformations and interactions favored in initial stages of folding, and in early intermediates formed during folding. We have characterized non-random structures favored in unfolded, redu...
Topics
- Amino Acid Sequence
- Animals
- Aprotinin
- Cattle
- Circular Dichroism
- Disulfides
- Genetic Variation
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Molecular Sequence Data
- Molecular Structure
- Mutagenesis, Site-Directed
- Protein Conformation
- Protein Denaturation
- Protein Folding