Article
The conformational stability of a non-covalent dimer of a platelet-derived growth factor-B mutant lacking the two cysteines involved in interchain disulfide bonds.
International journal of peptide and protein research - 1 Oct 1994
Prestrelski S J, Arakawa T, Duker K, Kenney W C, Narhi L O
Abstract excerpt
Native platelet-derived growth factor-B (PDGF-B) forms a covalent dimer through interchain disulfide bonds. In a previous study, an analog of PDGF-B was produced by replacing cysteine 43 and 52, which are involved in the interchain disulfide bonds, with serine. It was revealed that this analog protein has the dimeric molecule weight at pH 4 to 7, forming a non-covalent dimer in solution, and its mitogenic...
Topics
- Circular Dichroism
- Cystine
- Disulfides
- Drug Stability
- Guanidine
- Guanidines
- Mutation
- Platelet-Derived Growth Factor
- Protein Conformation
- Protein-Tyrosine Kinases