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Zygmunt S. Derewenda

Researcher at University of Virginia

Publications -  153
Citations -  13738

Zygmunt S. Derewenda is an academic researcher from University of Virginia. The author has contributed to research in topics: Protein structure & Protein crystallization. The author has an hindex of 61, co-authored 150 publications receiving 13169 citations. Previous affiliations of Zygmunt S. Derewenda include New York University & University of York.

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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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A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex

TL;DR: It is proposed that the structure of the enzyme in this complex of R. miehei lipase with n-hexylphosphonate ethyl ester is equivalent to the activated state generated by the oil–water interface.
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Overcoming Expression and Purification Problems of RhoGDI Using a Family of “Parallel” Expression Vectors☆

TL;DR: The development and use of expression vectors based on three of the most frequently used gene fusion affinity tags are discussed with respect to overcoming purification problems encountered for the RhoA GDP/GTP nucleotide dissociation inhibitor (RhoGDI) and their advantages over commercially available expression vectors.
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The occurrence of C-H...O hydrogen bonds in proteins.

TL;DR: This work describes an analysis of short C-H...O interactions in a sample of known protein structures representing different categories of tertiary folds and refined at a resolution of at least 2 A, and finds strong evidence that a large percentage of long C...O contacts constitute cohesive interactions.
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Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase.

TL;DR: The crystal structure of an extracellular triglyceride lipase inhibited irreversibly by diethyl p-nitrophenyl phosphate (E600) was solved by X-ray crystallographic methods and refined to a resolution of 2.65 A.