Liat Shimoni

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The modes of hydrogen bonding of arginine, asparagine, and glutamine side chains and of urea have been examined in small-molecule crystal structures in the Cambridge Structural Database and in crystal structures of protein-nucleic acid and protein-protein complexes. Analysis of the hydrogen bonding patterns of each by graph-set theory shows three patterns(More)
protLIMS is a web-based proteomics laboratory information management system. In February, we released version 1 of protLIMS, completed to the year one goal: The web-interface provides for recording of the biological material, protein mixture preparation, 2D-PAGE, gel image files and spot and plug mapping. Associated files may be uploaded and retrieved(More)
An analysis of the stereochemistry of hydrogen bonding and metal binding to some nitrogen-containing heterocycles found in crystal structure determinations has shown that the interacting atom will generally lie in the plane of the heterocyclic ring system in a direction that approximately bisects the C-N-C angle of the heterocycle. The Cambridge Structural(More)
Bovine porphobilinogen synthase (PBGS) is an homo-octameric enzyme with four active sites. Each active site binds two Zn(II) atoms whose ligands differ and two molecules of 5-aminolevulinate whose chemical fates differ. The asymmetric binding of two Zn(II) atoms and two identical substrate molecules by a homodimeric active site is apparently unique.(More)
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