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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 585 (1990), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 28 (1995), S. 829-834 
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: In order to directly observe the structure of enzyme intermediate complexes that form during turnover, one must ensure the homogeneous and complete accumulation of the intermediate during the collection of diffraction data. In the case of steady-state Laue experiments, the accumulation of the intermediate is dictated by the rate of substrate diffusion throughout the crystal, compared with the rate of turnover and disappearance of a rate-limited catalytic intermediate. This paper describes a simple quantitative method for measuring substrate diffusion and binding within an enzyme crystal. The set-up consists of a light source, specific bandpass filters, a crystallographic flow cell, a syringe pump, a charge-coupled-device color video camera and a workstation with a frame-grabber card for collection and digitization of images and subsequent processing of data. By this technique, any diffusion and binding process in a protein crystal leading to a visible absorbance shift may be accurately monitored and quantified during data collection. This method offers the crystallographer an inexpensive and simple alternative to the use of a single-crystal microspectrophotometer to measure the relatively slow process of diffusion.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 55 (1999), S. 1304-1326 
    ISSN: 1420-9071
    Keywords: Key words. Homing endonuclease; mobile intron; intein; crystallography.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. ‘Homing’ is the lateral transfer of an intervening genetic sequence, either an intron or an intein, to a cognate allele that lacks that element. The end result of homing is the duplication of the intervening sequence. The process is initiated by site-specific endonucleases that are encoded by open reading frames within the mobile elements. Several features of these proteins make them attractive subjects for structural and functional studies. First, these endonucleases, while unique, may be contrasted with a variety of enzymes involved in nucleic acid strand breakage and rearrangement, particularly restriction endonucleases. Second, because they are encoded within the intervening sequence, there are interesting limitations on the position and length of their open reading frames, and therefore on their structures. Third, these enzymes display a unique strategy of flexible recognition of very long DNA target sites. This strategy allows these sequences to minimize nonspecific cleavage within the host genome, while maximizing the ability of the endonuclease to cleave closely related variants of the homing site. Recent studies explain a great deal about the biochemical and genetic mechanisms of homing, and also about the structure and function of several representative members of the homing endonuclease families.
    Type of Medium: Electronic Resource
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