Article
pH driven fibrillar aggregation of the super-sweet protein Y65R-MNEI: A step-by-step structural analysis.
Biochimica et biophysica acta. General subjects - 1 Apr 2018
Pica Andrea, Leone Serena, Di Girolamo Rocco, Donnarumma Federica, Emendato Alessandro, Rega Michele Fortunato, Merlino Antonello, Picone Delia
Abstract excerpt
BACKGROUND: MNEI and its variant Y65R-MNEI are sweet proteins with potential applications as sweeteners in food industry. Also, they are often used as model systems for folding and aggregation studies. METHODS: X-ray crystallography was used to structurally characterize Y65R-MNEI at five different pHs, while circular dichroism and fluorescence spectroscopy were used to study their thermal and chemical stability....
Topics
- Circular Dichroism
- Crystallography, X-Ray
- Hydrogen-Ion Concentration
- Kinetics
- Microscopy, Atomic Force
- Models, Molecular
- Mutant Proteins
- Mutation
- Plant Proteins
- Protein Aggregates