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  • 1
    Electronic Resource
    Electronic Resource
    Structural principles for the propeller assembly of β-sheets: The preference for seven-fold symmetry (1992)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 14 (1992), S. 191-201 
    Details
    ISSN: 0887-3585
    Keywords: common protein fold ; protein architecture ; close packing ; p-sheet twist ; galactose oxidase ; influenza virus neuraminidase ; methylamine dehydrogenase ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Twisted β-sheets, packed face to face, may be arranged in circular formation like blades of a propeller or turbine. This β-pro-peller fold has been found in three proteins: that in neuraminidase consists of six β-sheets while those in methylamine dehydrogenase and galactose oxidase are composed of seven β-sheets. A model for multisheet packing in the β-propeller fold is proposed. This model gives both geometrical parameters of the β-propellers composed of different numbers of sheets and patterns of residue packing at their sheet-to-sheet interfaces. All the known β-propeller structures have been analyzed, and the observed geometries and residue packing are found to be in good agreement with those predicted by models. It is shown that unusual seven-fold symmetry is preferable to six- or eight-fold symmetry for propeller-like multisheet assembly. According to the model, a six β-sheet propeller has to have predominantly small residues in the β-strands closed to its sixfold axis, but no strong sequence constraints are necessary for a seven-fold β-propeller. © 1992 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340140206
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  • 2
    Electronic Resource
    Electronic Resource
    SCOP, Structural Classification of Proteins Database: Applications to Evaluation of the Effectiveness of Sequence Alignment Methods and Statistics of Protein Structural Data (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 1147-1154 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The Structural Classification of Proteins (SCOP) database provides a detailed and comprehensive description of the relationships of all known protein structures. The classification is on hierarchical levels: the first two levels, family and superfamily, describe near and far evolutionary relationships; the third, fold, describes geometrical relationships. The distinction between evolutionary relationships and those that arise from the physics and chemistry of proteins is a feature that is unique to this database, so far. The database can be used as a source of data to calibrate sequence search algorithms and for the generation of population statistics on protein structures. The database and its associated files are freely accessible from a number of WWW sites mirrored from URL http://scop.mrc-lmb.cam.ac.uk/scop/.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998009172
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  • 3
    Electronic Resource
    Electronic Resource
    Three sisters, different names (1994)
    [s.l.] : Nature Publishing Group
    Nature structural biology 1 (1994), S. 146-147 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Sir — The classical NAD binding fold, as seen in lactate dehydrogenase or liver alcohol dehydrogenases, consists of six strands of parallel β-pleated sheet flanked on either side by α-helices, with ∼100 structurally conserved residues1. Here, we report a novel subclass of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb0394-146
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  • 4
    Electronic Resource
    Electronic Resource
    PROTEIN FOLDS IN THE ALL-beta AND ALL-alpha CLASSES (1997)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biophysics and Biomolecular Structure 26 (1997), S. 597-627 
    Details
    ISSN: 1056-8700
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Physics
    Notes: Abstract Analysis of the structures in the Protein Databank, released in June 1996, shows that the number of different protein folds, i.e. the number of different arrangements of major secondary structures and/or chain topologies, is 327. Of these folds, approximately 25% belong to the all-alpha class, 20% belong to the all-beta class, 30% belong to the alpha/beta class, and 25% belong to the alpha + beta class. We describe the types of folds now known for the all-beta and all-alpha classes, emphasizing those that have been discovered recently. Detailed theories for the physical determinants of the structures of most of these folds now exist, and these are reviewed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.biophys.26.1.597
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  • 5
    Electronic Resource
    Electronic Resource
    A ribosomal protein module in EF-G and DNA gyrase (1995)
    [s.l.] : Nature Publishing Group
    Nature structural biology 2 (1995), S. 25-26 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Sir —Elongation factor G (EF-G) and DNA gyrase B are large multidomain proteins that control the intrinsic mechanical steps in complex biochemical reactions: EF-G in mRNA translation, and gyrase B in DNA supercoiling. Upon determination of their structures, it has been suggested that domain ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb0195-25
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  • 6
    Electronic Resource
    Electronic Resource
    Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9 (2002)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 416 (2002), S. 103-107 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Specific modifications to histones are essential epigenetic markers—heritable changes in gene expression that do not affect the DNA sequence. Methylation of lysine 9 in histone H3 is recognized by heterochromatin protein 1 (HP1), which directs the binding of other proteins to control ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature722
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  • 7
    Electronic Resource
    Electronic Resource
    Probable circular permutation in the flavin-binding domain (1998)
    [s.l.] : Nature Publishing Group
    Nature structural biology 5 (1998), S. 101-101 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Sir-Liepinsh et all have recently proposed an evolutionary link between electron transport and proteolysis based upon a structural relationship of the FMN binding protein (FMN-bp) from Desulfovibrio vulgaris (Miyazaki F) to chymotrypsin and related proteases. Having examined the sequence and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb0298-101
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  • 8
    Electronic Resource
    Electronic Resource
    Progress in protein structure prediction (2001)
    [s.l.] : Nature Publishing Group
    Nature structural biology 8 (2001), S. 110-112 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] “Now, here, you see, it takes all the running you can do, to keep in the same place. If you want to get somewhere else, you must run at least twice as fast as that!” The Red Queen to Alice in Through the Looking-Glass by Lewis Carroll Unlike many of the conferences in the past year, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/84088
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  • 9
    Electronic Resource
    Electronic Resource
    A protein catalytic framework with an N-terminal nucleophile is capable of self-activation (1995)
    [s.l.] : Nature Publishing Group
    Nature 378 (1995), S. 416-419 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The fold common to all three enzymes, illustrated schemat-ically in Fig. 1, is a four-layer a + P structure with two anti-parallel P-sheets, one essentially flat (I), the other slightly twisted (II). The P-sheets are packed in a unique arrangement in which one is rotated relative to the other ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/378416a0
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  • 10
    Electronic Resource
    Electronic Resource
    Familiar strangers (1992)
    [s.l.] : Nature Publishing Group
    Nature 360 (1992), S. 635-635 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR - All three protein structures1"3 reported in a recent issue of Nature display folding motifs previously observed in other protein structures. In only one case did the authors concerned notice this similarity. The amino-terminal domain in the staphylococcal enterotoxin B (SEE) structure1 ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/360635a0
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