Article
NMR spectroscopy of exchangeable protons of glucoamylase and of complexes with inhibitors in the 9-15-ppm range.
European journal of biochemistry - 1 Jul 1994
Firsov L M, Neustroev K N, Aleshin A E, Metzler C M, Metzler D E, Scott R D, Stoffer B, Christensen T, Svensson B
Abstract excerpt
1H-NMR spectra have been recorded for glucoamylases I and II from Aspergillus awamori var. X100 and from A. niger in the 9-15-ppm region. At least 17 distinct peaks, many of them arising from single protons, are observed. These are designated A-Q, A being the furthest downfield. At least 9 of these are lost rapidly by exchange when the enzyme is placed in D2O. Peaks A, B, E and H undergo distinct shifts with pH...
Topics
- Aspergillus
- Binding Sites
- Glucan 1,4-alpha-Glucosidase
- Magnetic Resonance Spectroscopy
- Mutation
- Protein Conformation
- Protons