Article
Reversible dissociation and unfolding of the Escherichia coli aspartate receptor cytoplasmic fragment.
Biochemistry - 7 Mar 1995
Wu J, Long D G, Weis R M
Abstract excerpt
The thermal denaturation of a 31-kDa soluble fragment derived from the Escherichia coli aspartate receptor cytoplasmic region (c-fragment) was found to be reversible. Denaturation monitored by differential scanning calorimetry (DSC) and circular dichroism (CD) was typically over 90% reversible in pH 7.0 buffer. The wild-type c-fragment exhibited one transition (Tm = 51 degrees C), which was taken as the main...
Topics
- Aspartic Acid
- Calorimetry, Differential Scanning
- Circular Dichroism
- Cytoplasm
- Escherichia coli
- Hot Temperature
- Mutation
- Peptide Fragments
- Protein Denaturation
- Protein Folding
- Receptors, Amino Acid