X-ray crystallographic analyses of complexes between bovine β-trypsin and schiff base copper(II) or iron(III) chelates11Edited by I. A. Wilson

Author:

Toyota Eiko,Ng Kenneth K.S,Sekizaki Horuo,Itoh Kunihiko,Tanizawa Kazutaka,James Michael N.G

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference32 articles.

1. Structure and specific binding of trypsin;Krieger;J. Mol. Biol,1974

2. The refined crystal structure of bovine β-trypsin at 1.8 Å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0;Bode;J. Mol. Biol,1975

3. The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors;Marquart;Acta Crystallog. sect. B,1983

4. Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density. Active site geometry, ion pairs and solvent structure;Bartunik;J. Mol. Biol,1989

5. Relocating a negative charge in the binding pocket of trypsin;Perona;J. Mol. Biol,1993

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