Journal
CHEMBIOCHEM
Volume 19, Issue 2, Pages 153-158Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201700596
Keywords
differential scanning calorimetry; enzymes; molecular modeling; small-angle X-ray scattering; solvent effects
Funding
- Cluster of Excellence RESOLV - Deutsche Forschungsgemeinschaft [EXC 1069]
- Boehringer Ingelheim Foundation (Plus-3 Program)
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3-Hydroxy-3-methylglutaryl-coenzymeA (HMG-CoA) reductase was investigated in different organic cosolvents by means of kinetic and calorimetric measurements, molecular dynamics simulations, and small-angle X-ray scattering. The combined experimental and theoretical techniques were essential to complement each other's limitations in the investigation of the complex interaction pattern between the enzyme, different solvent types, and concentrations. In this way, the underlying mechanisms for the loss of enzyme activity in different water-miscible solvents could be elucidated. These include direct inhibitory effects onto the active center and structural distortions.
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