Biomedical subjects
W Bode
Publications and source records attributed to W Bode.
[Intravital and postmortem measurements of coronary stenosis].
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Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin.
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Crystal structure of bovine trypsinogen at 1-8 A resolution. I. Data collection, application of patterson search techniques and preliminary structural interpretation.
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[Intravital and postmortem morphometry on coronary arteries].
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The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. I. Crystallization, data collection and application of patterson search technique.
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The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0.
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Involvement of tyrosine residues in the protomer-protomer interaction of Proteus mirabilis flagella as studied by spectroscopic methods, chemical modification and aggregation experiments.
Using spectrophotometrical titration, chemical modification, and ultraviolet difference spectral methods, the existence of at least two distinct tyrosine groups in the isolated flagellin of Proteus mirabilis flagella has been established. Three of the five flagellin tyrosines are buried in the protein matrix, whereas the other two seem to lie on the protein surface accessible to perturbants. Also about two tyrosine residues, presumably the latter ones exposed to the environment, can be nitrated with tetranitromethane in the monomeric flagellin with a concomitant loss of the polymerization ability after about one tyrosine per mol flagellin has been nitrated. Nitrated flagellin, homogeneous with respect to molecular weight, degree of nitration and isoelectric point, could be isolated and characterized. On the other hand, it could be shown that in the polymeric flagellum the phenolic groups of all five tyrosine residues are inaccessible to perturbing and modifying reagents. It seems, therefore, that the integrity of the phenolic groups is necessary for the proper folding and aggregation of the flagellin subunits to form the stable helical flagella.
The single calcium-binding site of crystallin bovin beta-trypsin.
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The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor III. Structure of the anhydro-trypsin-inhibitor complex.
The structure of the complex between anhydro-trypsin and pancreatic trypsin inhibitor has been determined by difference Fourier techniques using phases obtained from the native complex (Huber et al., 1974). It was refined independently by constrained crystallographic refinement at 1.9 A resolution. The anhydro-complex has Ser 195 converted to dehydro-alanine. There were no other significant structural changes. In particular, the high degree of pyramidalization of the C atom of Lys 15 (I) of the inhibitor component observed in the native complex in maintained in the anhydro-species.
Calorimetric studies on the in vitro polymerization of Pr. mirabilis flagellin.
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Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution.
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X-ray studies on antibody fragments.
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Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI.
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Functional classification of P22 amber mutants.
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Thermal transitions of Proteus mirabilis flagellin as studied by circular dichroism and adiabatic differential calorimetry.
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The bacterial flagella and the flagellar protein flagellin.
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A model of bacterial flagella based on small-angle x-ray scattering and hydrodynamic data which indicated an elongated shape of the flagellin protomer.
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