Folded ?-turns and collagenlike conformations of -Gly-Pro- and -Pro-Gly-sequences in synthetic polytripeptides
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چکیده
منابع مشابه
Oligopeptides with the sequences ala-pro-gly and gly-pro-gly as substrates or inhibitors for protocollagen proline hydroxylase.
Sequential oligopeptides prepared by condensation of peptides with the sequence Ala-Pro-Gly or Gly-Pro-Gly were examined as possible substrates or inhibitors for the synthesis of hydroxyproline by protocollagen proline hydroxylase. The tripeptide BOC-Ala-Pro-Gly-OMe (where BOC-represents 1-butoxycarboxyland Me represents methyl) was not hydroxylated, but oligopeptides ranging in size from BOC(A...
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The tetrapeptide Gly-Pro-Arg-Pro inhibits fibrinogen aggregation, probably by binding to the same sites used during initiation of fibrin formation. The Gly-Pro-Arg-Pro binding sites have not yet been identified. However, their possible sequence and locations have been predicted on the basis of the amino acid pairing hypothesis. One of these predicted sites is on fibrinopeptide A. We report here...
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Investigations determined the mechanism(s) by which Arg-Pro-Pro-Gly-Phe (RPPGF) inhibits thrombin-induced platelet activation. High concentrations of RPPGF inhibit thrombin-induced coagulant activity. RPPGF binds to the active site of thrombin by forming a parallel beta-strand with Ser214-Gly216 and interacts with His57, Asp189, and Ser195 of the catalytic triad. RPPGF competitively inhibits al...
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We report the first results from a new instrument capable of acquiring infrared spectra of mobility-selected ions. This demonstration involves using ion mobility to first separate the protonated peptide Gly-Pro-Gly-Gly (GPGG) into two conformational families with collisional cross-sections of 93.8 and 96.8 Å(2). After separation, each family is independently analyzed by acquiring the infrared p...
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ژورنال
عنوان ژورنال: Biopolymers
سال: 1984
ISSN: 0006-3525,1097-0282
DOI: 10.1002/bip.360230403