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Leo Brady

Researcher at University of Bristol

Publications -  8
Citations -  1959

Leo Brady is an academic researcher from University of Bristol. The author has contributed to research in topics: Virtual screening & Binding site. The author has an hindex of 7, co-authored 8 publications receiving 1918 citations.

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A serine protease triad forms the catalytic centre of a triacylglycerol lipase.

TL;DR: The X-ray structure of the Mucor miehei triglyceride lipase is reported and the atomic model obtained reveals a Ser .. His .. Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.
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Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus.

TL;DR: X-ray diffraction analysis of an acid alpha-amylase from Aspergillus niger allowed a detailed description of the stereochemistry of the calcium-binding sites, and a secondary binding site was identified at the bottom of the substrate binding cleft; it involves the residues presumed to play a catalytic role.
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A single amino acid residue can determine the sensitivity of SERCAs to artemisinins

TL;DR: It is shown that a single amino acid in transmembrane segment 3 of SERCAs can determine susceptibility to artemisinin, and an L263E replacement of a malarial by a mammalian residue abolishes inhibition by art Artemisinin.
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Structure and molecular model refinement of Aspergillus oryzae (TAKA) α‐amylase: an application of the simulated‐annealing method

TL;DR: The solution of the structure of this enzyme in a different crystal form, with only one molecule in the asymmetric unit is reported, using a model of acid alpha-amylase from a related fungus A. niger.