Tine E. Gottschalk

The Structure of Barley α-Amylase Isozyme 1 Reveals a Novel Role of Domain C in Substrate Recognition and Binding

Xavier Robert, Richard Haser, Tine E. Gottschalk et al. · Structure · 2003 · 141 citations · Full text

Cellular Enzymology, Biochemistry, Natural Sciences +6

Extensive N-Glycosylation Reduces the Thermal Stability of a Recombinant Alkalophilic Bacillus α-Amylase Produced in Pichia pastoris

Dedreia Tull, Tine E. Gottschalk, Ib Svendsen et al. · Protein Expression and Purification · 2001 · 41 citations

Biosynthesis, Engineering, Biocatalysis +9

Tyrosine 105 and Threonine 212 at Outermost Substrate Binding Subsites –6 and +4 Control Substrate Specificity, Oligosaccharide Cleavage Patterns, and Multiple Binding Modes of Barley α-Amylase 1

Kristian Sass Bak‐Jensen, Gwenaëlle André, Tine E. Gottschalk et al. · Journal of Biological Chemistry · 2004 · 40 citations · Full text

Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and −5/−6 of barley α‐amylase 1

Haruhide Mori, Kristian Sass Bak‐Jensen, Tine E. Gottschalk et al. · European Journal of Biochemistry · 2001 · 35 citations

Differences in conformational stability of barley alpha-amylase isozymes 1 and 2. Role of charged groups and isozyme 2 specific salt-bridges

Morten T. Jensen, Tine E. Gottschalk, Birte Svensson · Journal of Cereal Science · 2003 · 34 citations

Cellular Enzymology, Biochemistry, Protein Folding +8