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Johan P. Turkenburg

Researcher at University of York

Publications -  126
Citations -  8279

Johan P. Turkenburg is an academic researcher from University of York. The author has contributed to research in topics: Hydrolase & Glycoside hydrolase. The author has an hindex of 41, co-authored 124 publications receiving 7492 citations. Previous affiliations of Johan P. Turkenburg include New York University & Newcastle University.

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Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. family GH3 β-D-glucosidases.

TL;DR: The three-dimensional structures of two industrially important family GH3 β-d-glucosidases from A. fumigatus and A. oryzae are reported at 1.95 Å resolution, and both enzymes show extensive N-glycosylation.
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Non-equivalent Role of Inter- and Intramolecular Hydrogen Bonds in the Insulin Dimer Interface

TL;DR: All examined analogues crystallized only in the most stable R6 form of insulin oligomers (even if the dimer interface was totally disrupted), confirming the role of R6-specific intra/intermolecular interactions for hexamer stability.
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Insights into the structural determinants of cohesin-dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA.

TL;DR: The crystal structure of the Type II cohesin (CohII) is reported from the Clostridium thermocellum cell surface anchoring protein SdbA, which is very similar to Type I cohesins, and the dockerin binding site is likely to be conserved in the two proteins.
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Structural and functional analysis of the tandem β-zipper interaction of a streptococcal protein with human fibronectin

TL;DR: It is proposed that in SfbI-5, the binding energy for the tandem β-zipper interaction with Fn is distributed across the interface rather than concentrated in a small number of “hot spot” residues that are frequently observed in the interactions of folded proteins.
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Thermodynamic and structural investigation of the specific SDS binding of humicola insolens cutinase

TL;DR: The interaction of cutinase from the thermophilic fungus Humicola insolens with the anionic surfactant SDS is reported, and the enzyme specifically binds a single SDS molecule under nondenaturing concentrations.