309 research outputs found
Episode 5: Jim Bowyer
No full textRuntime 57:43In Episode 5, Eli interviews Jim Bowyer, professor emeritus at the University of Minnesota, senior contributor at Dovetail Partners, and author of The Irresponsible Pursuit of Paradise. Jim is well known for life cycle assessment research, designed to assess the environmental impact of a product or action by analyzing all of the component parts and processes. Jim offers insights about wood as a natural resource, the results of an environmental quiz that he has run for decades, and a critique of one of the most prominent environmental analyses ever conducted
York, England 1736
No full textSelected features shown pictorially.
Relief shown pictorially.
Includes indexes .
From: Eboracum : or, The history and antiquities of the city of York, from its original to the present times. Together with the history of the cathedral church, and the lives of the archbishops of that see. Collected from authentick manuscripts, publick records, ancient chronicles, and modern historians/ By Francis Drake, 1736.
"P. 244" -- upper left. Gift of Michael M. Katzman.1:6,00
‘The Great Bowyer Bible’: Robert Bowyer and the Macklin Bible
No full textThis article examines an iconic example of grangerizing: the Macklin Bible extra-illustrated in 45 volumes by London artist and bookseller Robert Bowyer (1758‐1834) in the first quarter of the nineteenth century (Bolton Libraries and Museums, Bolton, United Kingdom). The principal focus is on the Bowyer Bible as an example of an extra-illustrator’s close engagement with its source publication. The author argues that Bowyer’s practice responds not only to the Bible or the King James Bible, in general, but also to the Macklin Bible, in particular. The article discusses how the Bowyer Bible engages with the Macklin Bible specifically and how it reflects a broader range of concerns in its visual engagement with the Bible. It demonstrates that Bowyer’s curation of biblical visual material evidences both his professional interests as a connoisseur of prints and his personal interests in the visual culture of the Bible that reflect his own piety as well as contemporaneous developments in the study of the scriptures. Other matters discussed in the article are the original function of this Bible, as well as the extent to which it reflects and is distinctive from contemporaneous extra-illustrated books
The unequal match [electronic resource] : a tale. By the author of The curious maid.
No full textAuthor of 'The curious maid' = Hildebrand Jacob.Verse.Printed by William Bowyer; his records show 100 copies printed (apparently a reimpression rather than a new edition).Signatures: [A]p2s Bp2s.Signatures from Maslen & Lancaster, and Foxon.Foxon,Maslen & Lancaster. Bowyer ledgers,Electronic reproduction.English Short Title Catalog,Reproduction of original from Harvard University Houghton Library
Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis
No full textThe X-ray structure of the holo-form of l-threonine dehydrogenase (TDH) from Thermococcus kodakaraensis (TkTDH) has been determined at 2.4 Å resolution. TDH catalyses the NAD+-dependent oxidation of l-threonine to 2-amino-3-ketobutyrate, and is one of the first enzymes in this family to be solved by X-ray crystallography. The enzyme is a homo-tetramer, each monomer consisting of 350 amino acids that form two domains; a catalytic domain and a nicotinamide co-factor (NAD+)-binding domain, which contains an ?/? Rossmann fold motif. An extended twelve-stranded ?-sheet is formed by the association of pairs of monomers in the tetramer. TkTDH shows strong overall structural similarity to TDHs from thermophiles and alcohol dehydrogenases (ADH) from lower life forms, despite low sequence homology, exhibiting the same overall fold of the monomer and assembly of the tetramer. The structure reveals the binding site of the essential co-factor NAD+ which is present in all subunits. Docking studies suggest a mode of interaction of TDH with 2-amino-3-ketobutyrate CoA ligase, the subsequent enzyme in the pathway for conversion of threonine to glycine. TDH is known to form a stable functional complex with 2-amino-3-ketobutyrate ligase, most probably to shield an unstable intermediate
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