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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Research in engineering design 9 (1997), S. 85-98 
    ISSN: 1435-6066
    Keywords: CAD ; Collaboration ; Databases ; Design
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Technology
    Notes: Abstract Collaborative design is currently supported through the integration of graphical representations with relational databases and the distribution of data and applications across local and wide area networks. Recent developments in computer support for synchronous collaboration have led to the development of multi-user drawing boards and video conferencing software for remote meetings. The extension of CAD for use in a collaborative design session changes the focus of collaborative design from a distribution of data to a shared workspace. Combining CAD with the concept of multi-user software introduces issues of shared visualisation and shared decision making. A model for the integration of CAD and database management in a collaborative design session is presented within a client server architecture, and an implementation of this model using AutoCAD as the shared CAD system is described.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1327
    Keywords: Key words Reduction potential ; Rubredoxin ; Square wave voltammetry ; X-ray crystallography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The Pri sidechains of two adjacent valine residues, V8 and V44, define the surface of the rubredoxin from Clostridium pasteurianum and control access to its Fe(S-Cys)4 active site. To assess the effect of systematic change of the steric bulk of the alkyl sidechains, eight single and three double mutant proteins have been isolated which vary G (H), A (Me), V (Pri), L (Bui) and I (Bus) at those positions. X-ray crystal structures of the FeIII forms of the V44A and V44I proteins are reported. Positive shifts in reversible potential of up to 116 mV are observed and attributed to increased polarity around the Fe(S-Cys)4 site induced by (1) changes in protein backbone conformation driven by variation of the steric demands of the sidechain substituents and (2) changes in solvent access to the sidechains of ligands C9 and C42. Data for the V44A mutant show that a minor change in the steric requirements of a surface residue can introduce a NH···Sγ hydrogen bond at the active site and lead to a shift in potentialof +50 mV.
    Type of Medium: Electronic Resource
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