The preferred conformation of the tripeptide Ala-Phe-Ala in water is an inverse g-turn: implications for protein folding and drug design (Articolo in rivista)

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  • The preferred conformation of the tripeptide Ala-Phe-Ala in water is an inverse g-turn: implications for protein folding and drug design (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/bi050658v (literal)
Alternative label
  • MOTTA, A.; Reches, M.; Pappalardo, L.; Andreotti, G.; Gazit, E. (2005)
    The preferred conformation of the tripeptide Ala-Phe-Ala in water is an inverse g-turn: implications for protein folding and drug design
    in Biochemistry (Easton)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • MOTTA, A.; Reches, M.; Pappalardo, L.; Andreotti, G.; Gazit, E. (literal)
Pagina inizio
  • 14170 (literal)
Pagina fine
  • 14178 (literal)
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  • 44 (literal)
Rivista
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  • 43 (literal)
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  • Analisi NMR di un tripeptide che presenta una insolita struttura ben definita. Potenziali applicazioni nel drug design. (literal)
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  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
  • PubMe (literal)
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  • Istituto di Chimica Biomolecolare del CNR, Comprensorio OliVetti, Edificio A, Via Campi Flegrei 34, I-80078 Pozzuoli (Napoli), Italy; Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel AViV UniVersity, Tel AViV 69978, Israel (literal)
Titolo
  • The preferred conformation of the tripeptide Ala-Phe-Ala in water is an inverse g-turn: implications for protein folding and drug design (literal)
Abstract
  • Recent studies have provided evidence that peptides as short as tripeptides do adopt preferred conformations. Here we report that the tripeptide Ala-Phe-Ala (AFA) in aqueous solution preferentially forms an inverse Á-turn. Circular dichroism (CD) indicated the presence of a predominant turn structure, and Fourier transform infrared (FTIR) bands suggested the presence of a g-turn forming a bifurcated H-bond with the solvent molecules. The high-resolution structure was obtained by a combined use of NMR spectroscopy and calculations. On the basis of 30 unambiguous ROESY-derived distance restraints (including the Ha-NH NOE between Ala1 and Ala3 and a hydrogen bond between the CO group of Ala1 and the NH group of Ala3), calculations clearly demonstrated the presence of an inverse g-turn centered on Phe2. From NOE data, we estimated a mole fraction for the g-turn of 0.65. Since for AFA an extended b-strand was also reported [Eker, F., Griebenow, K., Cao, X., Nafie, L. A., and Schweitzer-Stenner, R. (2004) Proc. Natl. Acad. Sci. U.S.A. 101, 10054-10059], we investigated the possibility that g-turn and‚-strand may represent two major conformations. By using a best-fit procedure that calculated experimental NOEs as weighted averages of the effects originating from both structures, we were able to calculate with good accuracy the backbone NOEs at 280 K in terms of the two limiting conformers, yielding a mole fraction for the Á-turn and ‚-strand conformations of 0.60 and 0.40, respectively, in good agreement with those found by NOE data. The implication of the existence of a preferred conformation by a small structural element is discussed in the context of the nucleation of protein folding events and the design of small peptide and peptidomimetic drugs. (literal)
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