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  • 1
    Electronic Resource
    Electronic Resource
    Larval release in brachyuran crustaceans Functional similarity of peptide pheromone receptor and catalytic site of trypsin (1990)
    Springer
    Journal of chemical ecology 16 (1990), S. 1359-1370 
    Details
    ISSN: 1573-1561
    Keywords: Rhithropanopeus harrisii ; crab ; Crustacea ; larval release pheromone ; peptide pheromone ; trypsin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Studies of crab egg hatching and larval release behavior in the crab,Rhithropanopeus harrisii, generated a model describing the process. In the model, carboxyl terminal arginine peptides serve as pheromones that synchronize larval release. In response to the peptides, the female performs Stereotypic larval release behavior and casts larvae into the water column. The peptides originate from trypsin-like enzymatic activity as part of the egghatching process. Hatching can be simulated experimentally by incubating ovigerous crabs in either bovine or porcine trypsin. The female performs the larval release behavior. Eggs detach from the female, and immobile larvae hatch prematurely. Preincubation of trypsin with trypsin inhibitors eliminates these effects. Approximately nanomolar concentrations of five different polypeptide trypsin inhibitors evoke the female's larval release behavior. Because both peptides and trypsin inhibitors evoke larval release behavior and because trypsin inhibitors bind to both the peptide receptor and the enzyme with high affinity, the receptor binding site and trypsin catalytic site must be very similar. A relationship between the binding site of a peptide receptor and the catalytic site of trypsin is postulated. The difference may be substitution by a basic amino acid for the catalytic site serine. Molecular graphics modeling indicates that all necessary conditions for receptor binding can be met by substitution with lysine for the active site serine in the trypsin catalytic site. This substitution eliminates catalytic activity, maintains the binding affinity for trypsin inhibitors, and increases binding strength for peptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01021032
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Synthesis of an iron(II)-braced proline-II tripod protein (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 33-43 
    Details
    ISSN: 1573-3904
    Keywords: 4-amino-l-proline ; circular dichroic spectropolarimetry ; proline-II helix ; protein engineering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary This paper describes the engineering of braced tripod proteins for use as molecular frameworks. Specifically, a 30-residue tripod-shaped protein with three proline-II helical legs braced by an iron(II)tris(bipyridine) complex was modularly designed, chemically synthesized, and biophysically characterized. Three copies of a 10-residue leg peptide were covalently linked through sulfide bonds to an N-terminal apex (1,3,5-tris(methylene)benzene) and by amide bonds to the brace (FeII (Mbc)3: Mbc is 4′-methyl-2,2′-bipyridine-4-carbonyl). The leg peptide (H-Cys-Pro5-Pra(Mbc)-Pro3-NH2: Pra iscis-4-amino-l-proline) was assembled by the solid-phase method using Boc-Pra(Mbc)-OH, which was synthesized in 75% overall yield by coupling Mbc-OH to the 4-amino group of Boc-Pra-OCH3 and saponifying the methyl ester group. The iron(II)-braced tripod was assembled by S-alkylation of three copies of the leg peptide with 1,3,5-tris(bromomethyl)benzene followed by ligation of Fe2+ to the resulting unbraced tripod. The CD spectrum of the iron(II)-braced tripod showed a positive MLCT band at 570 nm and a negative π-π* band at 312 nm, so its FeII(Mbc)3 brace was predominantly in the Δ configuration. In a mostly acetonitrile solution at 25°C, the leg peptide and the unbraced tripod isomerized from the proline-II helical form into the proline-I helical form but the iron(II)-braced tripod remained in the proline-II helical form.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443616
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Synthesis of an iron(II)-braced proline-II tripod protein (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 33-43 
    Details
    ISSN: 1573-3904
    Keywords: 4-amino-l-proline ; circular dichroic spectropolarimeter ; proline-II helix ; protein engineering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract This paper describes the engineering of braced tripod proteins for use as molecular frameworks. Specifically, a 30-residue tripod-shaped protein with three proline-II helical legs braced by an iron(II)tris(bipyridine) complex was modularly designed, chemically synthesized, and biophysically characterized. Three copies of a 10-residue leg peptide were covalently linked through sulfide bonds to an N-terminal apex (1,3,5-tris(methylene)benzene) and by amide bonds to the brace (FeII(Mbc)3: Mbc is 4′-methyl-2,2′-bipyridine-4-carbonyl). The leg peptide (H-Cys-Pro5-Pra(Mbc)-Pro3-NH2: Pra is cis-4-amino-l-proline) was assembled by the solid-phase method using Boc-Pra(Mbc)-OH, which was synthesized in 75% overall yield by coupling Mbc-OH to the 4-amino group of Boc-Pra-OCH3 and saponifying the methyl ester group.The iron(II)-braced tripod was assembled by S-alkylation of three copies of the leg peptide with 1,3,5-tris(bromomethyl)benzene followed by ligation of Fe2+ to the resulting unbraced tripod. The CD spectrum of the iron(II)-braced tripod showed a positive MLCT band at 570 nm and a negative π–π* band at 312 nm, so its FeII(Mbc)3 brace was predominantly in the Δ configuration. In a mostly acetonitrile solution at 25 °C, the leg peptide and the unbraced tripod isomerized from the proline-II helical form into the proline-I helical form but the iron(II)-braced tripod remained in the proline-II helical form.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008863326742
    Location Call Number Limitation Availability
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    Paper (German National Licenses)
    Fulltext
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