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Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds.
The crystal structure of the isoform PsTI-IVb was determined by molecular replacement at 2.7 A resolution using the X-ray co-ordinates of the soybean inhibitor as a search model and the inhibitor crystallized with a nearly perfect 2-fold symmetric dimer in the asymmetric unit.
X-ray structure of TMP kinase from Mycobacterium tuberculosis complexed with TMP at 1.95 A resolution.
A complete multialignment of all known sequences of TMP kinases is presented and Subtle differences in the TMP binding site were noted, as compared to the Escherichia coli, yeast and human enzyme structures, which could be used to design specific inhibitors of this essential enzyme of nucleotide metabolism.
The Multiwavelength Anomalous Solvent Contrast (MASC) Method in Macromolecular Crystallography.
The main steps of a MASC experiment are discussed in the context of a MAD-like data collection optimized for accurate measurements of intensities of anomalous pairs at low resolution and the results of preliminary experiments on two protein crystals are reported.
The highly similar TMP kinases of Yersinia pestis and Escherichia coli differ markedly in their AZTMP phosphorylating activity.
To characterize the TMP kinase of Yersinia pestis, a chromosomal region encompassing its gene was cloned and sequenced; a high degree of conservation with the corresponding region of Escherichia coli was found.
Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis.
The protein p64k from the surface of the Neisseria meningitidis bacteria has been characterized as a two-domain protein. It contains a dihydrolipoamide dehydrogenase domain of 482 residues, involving
Protein flexibility and aggregation state of human epidermal growth factor. A time-resolved fluorescence study of the native protein and engineered single-tryptophan mutants.
A time-resolved fluorescence spectroscopic study of the recombinant human epidermal growth factor (hEGF) and of the two single-tryptophan-containing engineered mutants with Trp49 or Trp50 replaced by Phe, demonstrates the existence of a dimerization process of the native protein which is dependent on pH and protein concentration.
Substrate-induced fit of the ATP binding site of cytidine monophosphate kinase from Escherichia coli: time-resolved fluorescence of 3'-anthraniloyl-2'-deoxy-ADP and molecular modeling.
These results provide the first experimental arguments about an ATP-mediated induced-fit of the LID in CMPK(coli) modulated by CMP, leading to a closed conformation of the active site, protected from water.
Time-resolved fluorescence study of human recombinant interferon alpha 2. Association state of the protein, spatial proximity of the two tryptophan residues.
Close proximity of the two Trp residues (less than 1 nm) is suggested from steady-state and time-resolved fluorescence-anisotropy measurements in vitrified medium, in agreement with the recently published three-dimensional structure of the homologous protein murine interferon beta.
Crystallization and preliminary X-ray investigation of a recombinant outer membrane protein from Neisseria meningitidis.
A protein constituent of the outer membrane from Neisseria meningitidis (hereafter called P64K) has been crystallized using the hanging drop technique, indicating that a high resolution structure analysis is feasible.
Insight into the activation mechanism of Bordetella pertussis adenylate cyclase by calmodulin using fluorescence spectroscopy.
The interaction of the adenylate cyclase catalytic domain (AC) of the Bordetella pertussis major exotoxin with its activator calmodulin (CaM) was studied by time-resolved fluorescence spectroscopy