Article
A Conserved Tryptophan (Trp10) at the Hydrophobic Core Modulates the Stability and Inhibitory Activity of Potato I Type Inhibitors.
Protein and peptide letters - 1 Jan 2024
Cui Xiaodong, Shen Jiahui, Wang Jiajie, Li Chen, Li Fang, Li Jiao
Abstract excerpt
BACKGROUND: Different inhibitor families have their own conserved three-dimensional structures, but how these structures determine whether a protein can become an inhibitor is still unknown. The buckwheat trypsin inhibitor (BTI) pertains to the Potato I type inhibitor family, which is a simple and essential bio-molecule that serves as a model for the investigation of protease-inhibitor interaction. OBJECTIVE: To...
Topics
- Hydrophobic and Hydrophilic Interactions
- Tryptophan
- Mutagenesis, Site-Directed
- Plant Proteins
- Solanum tuberosum
- Trypsin Inhibitors
- Models, Molecular
- Hydrogen Bonding
- Protein Stability
- Trypsin
- Mutation
- Amino Acid Sequence