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  • 1990-1994  (5)
  • 1
    Electronic Resource
    Electronic Resource
    A human cDNA coding for the Leydig insulin-like peptide (Ley I-L) (1994)
    Springer
    Human genetics 〈Berlin〉 94 (1994), S. 91-94 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract cDNA clones for the human Leydig insulin-like peptide (Ley I-L) have been isolated and characterized. The nucleotide sequence of the 743-bp cDNA includes an incomplete 7-bp 5′-noncoding region, an open reading frame of 393 bp, and a 343-bp 3′-noncoding region. By primer extension analysis, the transcription start site was determined as being 14-bp upstream of the translation start site. The underlying gene is expressed in the testis but not in other organs. From the cDNA sequence, it can be deduced that the Ley I-L protein is synthesized as a 131-amino-acid (aa) preproprotein and that it contains a 24-aa signal peptide. Comparison of the pro Ley I-L protein with members of the insulin-like hormone superfamily predicts that the biologically active hormone, after proteolytic processing of the C peptide, consists of a 31-aa long B chain and a 26-aa long A chain, and that it has a molecular weight of 6.25 kDa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02272850
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Reconstruction of symmetry-related molecules from protein data bank (PDB) files (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 27 (1994), S. 1006-1009 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Many natural proteins are active as multimers. Crystallographic protein databases, however, generally store only part of the native multimer, the asymmetric unit, along with symmetry information. As a result of inaccuracies in the data, it is not always possible to reconstruct the native multimer. Here, a set of methods is presented that are designed to cope with inconsistencies in symmetry information. Applications include the validation of Protein Data Bank entries and the automatic generation of symmetry contacts for inspection and analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889894007764
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Quality control of protein models: directional atomic contact analysis (1993)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 26 (1993), S. 47-60 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Branden & Jones state, in Nature: `Protein crystallography is an exacting trade, and the results may contain errors that are difficult to identify. It is the crystallographer's responsibility to make sure that incorrect protein structures do not reach the literature.' [Branden & Jones. (1990). Nature (London), 343, 687–689.] One of several available methods of checking structures for correctness is the evaluation of atomic contacts. From an initial hypothesis that atom-atom interactions are the primary determinant of protein folding, any protein model can be tested for proper packing by the calculation of a contact quality index. The index is a measure of the agreement between the distributions of atoms around each residue fragment in the model and equivalent distributions derived from the database of known structures solved at high resolution. The better the agreement, the higher the contact quality index. This empirical test, which is independent of X-ray data, is applied to a series of successively refined crystal structures. In all cases, the model known or expected to be better (the one with the lower R-factor) has a better contact quality index, indicating that this type of contact analysis can be used as an independent quality criterion during crystallographic refinement. Modelled proteins and predicted mutant structures can also be evaluated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889892008240
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The structure of ColE1 rop in solution (1991)
    Springer
    Journal of biomolecular NMR 1 (1991), S. 71-82 
    Details
    ISSN: 1573-5001
    Keywords: rop ; Protein conformation ; 2D NMR ; Molecular dynamics ; Repressor proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The structure of the ColE1 repressor of primer (rop) protein in solution was determined from the proton nuclear magnetic resonance data by a combined use of distance geometry and restrained molecular dynamics calculations. A set of structures was determined with low internal energy and virtually no violations of the experimental distance restraints. Rop forms homodimers: Two helical hairpins are arranged as an antiparallel four helix bundle with a left-handed rope-like twist of the helix axes and with left-handed bundle topology. The very compact packing of the side chains in the helix interfaces of the rop coiled-coil structure may well account for its high stability. Overall, the solution structure is highly similar to the recently determined X-ray structure (Banner, D.W., Kokkinidis, M. and Tsernoglou, D. (1987)J. Mol. Biol.,196, 657–675), although there are minor differences in regions where packing forces appear to influence the crystal structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01874570
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of rhodanese (1990)
    Springer
    Journal of molecular histology 22 (1990), S. 197-200 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The role of rhodanese in the detoxication of acute cyanide exposure is controversial. The debate involves questions of the availability of rhodanese to cyanide in the peripheral circulation. Blood-borne cyanide will distribute to the brain and may induce lesions or even death. The present study addresses the dispute by determining the distribution of rhodanese in tissues considered to have the highest rhodanese activity and thought to serve as major detoxication sites. The results indicate that rhodanese levels are highest in (1) hepatocytes that are in close proximity to the blood supply of the liver (2) epithelial cells surrounding the bronchioles (a major entry route for gaseous cyanide) and (3) proximal tubule cells of the kidney (serving to facilitate cyanide detoxication and elimination as thiocyanate). Rhodanese activity in the brain is low compared with liver and kidney (Mimoriet al., 1984; Drawbaugh & Marrs, 1987); the brain is not considered to be a major site of cyanide detoxication. The brain, however, is the target for cyanide toxicity. In this study our goal was also to differentiate the distribution of rhodanese in an area of the brain. We found that the enzyme level is highest in fibrous astrocytes of the white matter. Cyanide-induced brain lesions may thus occur in areas of the brain lacking sufficient sites for detoxication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02386005
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    Paper (German National Licenses)
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