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  • 1
    Electronic Resource
    Electronic Resource
    Calorimetric studies on thein vitro polymerization ofPr. mirabilis flagellin (1974)
    Springer
    European biophysics journal 1 (1974), S. 55-64 
    Details
    ISSN: 1432-1017
    Keywords: Calorimetry ; Circular Dichroism ; Flagellin ; Polymerization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The heat effects accompanying the isothermalin vitro polymerization ofPr. mirabilis flagellin on short flagella fragments (seeds) have been measured in phosphate buffer pH 7, at various temperatures employing a batch microcalorimeter. Additionally, at 20
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01022560
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary x-ray diffraction data of the cryptomonad biliprotein phycocyanin-645 from a Chroomonas spec. (1984)
    Springer
    Archives of microbiology 140 (1984), S. 202-205 
    Details
    ISSN: 1432-072X
    Keywords: Chroomonas ; Cryptomonad biliprotein ; Crystallization ; Phycocyanin-645 ; Protein crystallography ; X-ray diffraction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The water-soluble antenna chromoprotein phycocyanin-645 from a Chroomonas species (Cryptophyceae) has been crystallized. X-ray precession photographs prove space groups P3121 (or the enantiomorphic P3221) for the trigonal and P212121 for the orthorhombic crystals. Density measurements indicate that the asymmetric units of these crystals contain three or two heterotetrameric units (αάβ 2), respectively. The packing of both crystal forms is quite different to that of any other crystals reported so far for phycobiliproteins of blue-green and red algae. The cationic detergent benzalkonium chloride (BAC) is strongly bound in the crystals. Both observations indicate a considerable membrane affinity and a unique association behaviour of the phycobiliproteins from cryptomonads.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00454927
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  • 3
    Electronic Resource
    Electronic Resource
    Expression, Purification, Characterization, and X-Ray Analysis of Selenomethionine 215 Variant of Leukocyte Collagenase (1997)
    Springer
    The protein journal 16 (1997), S. 637-650 
    Details
    ISSN: 1573-4943
    Keywords: Matrix metalloproteinases ; Met-turn ; Selenomethionine ; conformational stability ; X-ray crystallography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Matrix metalloproteinases belong to the superfamily of metzincins containing, besides a similar topology and a strictly conserved zinc environment, a 1,4-tight turn with a strictly conserved methionine residue at position three (the so called Met-turn [Bode et al. (1993) FEBS 331, 134–140; Stöcker et al. (1995) Protein Sci. 4, 823–840]. The distal S–CH3 moiety of this methionine residue forms the hydrophobic basement of the three His residues liganding the catalytic zinc ion. To assess the importance of this methionine, we have expressed the catalytic domain of neutrophil collagenase (rHNC, residues Met80–Gly242) in the methionine auxotrophic Escherichia coli strain B834[DE3](hsd metB), with the two methionine residues replaced by Selenomethionine. Complete replacement was confirmed by amino acid analysis and electrospray mass spectrometry. The folded and purified enzyme retained its catalytic activity, but showed modifications which are reflected in changed kinetic parameters. The Met215SeMet substitution caused a decrease in conformational stability upon urea denaturation. The X-ray crystal structure of this Selenomethionine rHNC was virtually identical to that of the wild-type catalytic domain except for a very faint local disturbance around the sulfur-seleno substitution site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026327125333
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  • 4
    Electronic Resource
    Electronic Resource
    Aktivierung, Aktivität und Inhibierung des Rindertrypsins (1979)
    Springer
    Naturwissenschaften 66 (1979), S. 251-258 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Notes: Abstract Trypsin is a prototype of a large group of enzymes belonging to serine proteinases. The X-ray crystal-structure analyses of its proenzyme trypsinogen, of the active trypsin and of their complexes formed with the pancreatic trypsin inhibitor (PTI) have considerably enhanced our understanding of the mechanisms of activitation, action and inhibition. The trypsinogen is an incompletely folded molecule. Its substrate-binding site becomes only completely fixed upon the enzymatic cleavage of an N-terminal peptide. The contact regions of trypsin and PTI are almost complementary. The complex formed is a (stable) intermediate in the normal tryptic substrate-cleavage reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00571605
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  • 5
    Electronic Resource
    Electronic Resource
    Crystal structures of thrombin and thrombin complexes as a framework for antithrombotic drug design (1994)
    Springer
    Perspectives in drug discovery and design 1 (1994), S. 431-452 
    Details
    ISSN: 1573-9023
    Keywords: Thrombin ; Fibrinogen ; Hirudin ; Heparin ; Drug design ; Crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The wealth of structural information now available on thrombin, its precursors, its substrates and its inhibitors allows a rationalization of its many roles. α-Thrombin exhibits an unusually deep and narrow active-site cleft, formed by loop insertions that are characteristic of thrombin. This canyon structure is one of the prime causes for the narrow specificity of thrombin. As a result of the conjunction of amino acid residues with similar properties such as charge or hydrophobicity, thrombin can be divided up into a number of functional regions. The apposition of the active site to a hydrophobic pocket (the apolar binding site) on one side and a basic patch (the fibrinogen recognition exosite) on the other allows for a fine-tuning of enzymatic activity, as seen for fibrinogen. These two sites are also optimally used by the leech-derived inhibitor hirudin, allowing the very tight binding observed; thrombin inhibition is effected by blocking access to the active site. Interactions with antithrombin III are tightened with the help of heparin, which binds to a second basic site (the heparin binding site). Non-proteolytic cellular properties are attributed to the rigid insertion loop at Tyr60A. The observed rigidity of the thrombin molecule in its complexes makes thrombin ideal for structure-based drug design. Thrombin can be inhibited either at the active site or at the fibrinogen recognition exosite, or both. Structural information shows that binding at the former is enhanced by good fit of aromatic moieties to the aryl and S2 binding sites (the apolar binding site). Binding at the fibrinogen recognition exosite is facilitated by negatively charged groups. The unpredictable nature of inhibitor binding underlines the importance of experimental monitoring of structures of thrombin inhibitors in the drug design process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02171858
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