ORCID Profile
0000-0002-6328-7200
Current Organisation
University of Leeds
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Publisher: American Chemical Society (ACS)
Date: 07-01-2011
DOI: 10.1021/JE100999J
Publisher: Walter de Gruyter GmbH
Date: 07-09-2011
Abstract: ThermoML is an XML-based approach for storage and exchange of experimental, predicted, and critically evaluated thermophysical and thermochemical property data. Extensions to the ThermoML schema for the representation of speciation, complex equilibria, and properties of biomaterials are described. The texts of 14 data files illustrating the new extensions are provided as Supplementary Information together with the complete text of the updated ThermoML schema.
Publisher: Portland Press Ltd.
Date: 08-2002
DOI: 10.1042/BJ20020168
Abstract: We previously reported on the xylanase-inhibiting protein I (XIP-I) from wheat [McLauchlan, Garcia-Conesa, Williamson, Roza, Ravestein and Maat (1999), Biochem. J. 338, 441–446]. In the present study, we show that XIP-I inhibits family-10 and −11 fungal xylanases. The Ki values for fungal xylanases ranged from 3.4 to 610nM, but bacterial family-10 and −11 xylanases were not inhibited. Unlike many glycosidase inhibitors, XIP-I was not a slow-binding inhibitor of the Aspergillus niger xylanase. Isothermal titration calorimetry of the XIP-I—A. niger xylanase complex showed the formation of a stoichiometric (1:1) complex with a heat capacity change of −1.38kJ·mol−1·K−1, leading to a predicted buried surface area of approx. 2200±500Å2 at the complex interface. For this complex with A. niger xylanase (Ki = 320nM at pH 5.5), titration curves indicated that an observable interaction occurred at pH 4–7, and this was consistent with the pH profile of inhibition of activity. In contrast, the stronger complex between A. nidulans xylanase and XIP-I (Ki = 9nM) led to an observable interaction across the entire pH range tested (3–9). Using surface plasmon resonance, we show that the differences in the binding affinity of XIP-I for A. niger and A. nidulans xylanase are due to a 200-fold lower dissociation rate koff for the latter, with only a small difference in association rate kon.
Publisher: Elsevier BV
Date: 05-2001
Location: United States of America
Location: United States of America
Location: United States of America
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
Location: No location found
No related grants have been discovered for John Ladbury.