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The solution conformation of the luteinizing hormone-releasing hormone (LHRH) anti-sense and reversed anti-sense peptides

Otter, Albin ; Scott, Paul G ; Stewart, John M ; Kotovych, George

Canadian journal of chemistry, 1990-07-01, Vol.68 (7), p.1083-1091 [Periódico revisado por pares]

Ottawa, Canada: NRC Research Press

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  • Título:
    The solution conformation of the luteinizing hormone-releasing hormone (LHRH) anti-sense and reversed anti-sense peptides
  • Autor: Otter, Albin ; Scott, Paul G ; Stewart, John M ; Kotovych, George
  • Assuntos: Atomic and molecular physics ; Exact sciences and technology ; Molecular properties and interactions with photons ; Physics
  • É parte de: Canadian journal of chemistry, 1990-07-01, Vol.68 (7), p.1083-1091
  • Descrição: The LHRH anti-sense peptide (Ser 1 -Arg 2 -Ala 3 -Gln 4 -Ser 5 -Ile 6 -Gly 7 -Pro 8 -Val 9 -Leu 10 ) and the inversed sequence, the LHRH inversed anti-sense peptide, have been studied by 1 H and 13 C NMR in one and two dimensions. The spectroscopic evidence, obtained in CD 3 OH/H 2 O (60/40) solution at pH 3.6, indicates that the first four amino acids of the anti-sense peptide form one complete 3 10 -helical turn followed by an extended conformation for the rest of the peptide. On the time-averaged NMR scale the molecules in the 3 10 -helical conformation are in fast exchange with the molecules that are extended throughout (major conformer). The reversed anti-sense peptide exhibits less discernible features. It appears likely that a small percentage of the molecules form a β-turn in the C-terminal four residues. Another β-turn might be located in the Val 2 -Ile 5 fragment. Both turns occur in very minor concentrations only, and therefore it is impossible to define what kind of β-turns are present. Keywords: LHRH anti-sense, inversed anti-sense, conformation, NMR.
  • Editor: Ottawa, Canada: NRC Research Press
  • Idioma: Inglês

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