Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects.

Abstract : 2-D and 3-D NMR techniques were used to investigate the conformations in solution of several peptides and proteins for which crystalline structures are not available yet. Insect defensin A is a small (40 aa) antibiotic protein exhibiting a characteristic 'loop-helix-beta-sheet' structure. A striking analogy was found with charybdotoxin, a scorpion toxin in which a CSH (cysteine stabilized alpha-helix) motif is also present. Wheat phospholipid transfer protein (PLTP) (90 aa) has a 3-D structure resulting from the packing of four helices and of a C-terminal less well-defined fragment. Preliminary results show that PLTP forms a complex with lyso-PC and that such an interaction results in a conformational change affecting principally the C-terminal half of the protein. A last example is given with surfactin, a lipopeptide biosurfactant from bacterial origin. Its protonated form shows a very compact structure in which the two acidic residues located on the top of a 'horse saddle' topology face each other, whereas the ionized form could adopt a more extended conformation. A common property of these compounds is their capacity to interact with lipids. The present structural data open the way for a further establishment of structure-activity relationships.
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Journal articles
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https://hal.archives-ouvertes.fr/hal-00433186
Contributor : Marie-Christine Averlant-Petit <>
Submitted on : Wednesday, November 18, 2009 - 1:45:53 PM
Last modification on : Monday, September 23, 2019 - 3:32:04 PM

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  • HAL Id : hal-00433186, version 1
  • PUBMED : 1467342

Citation

J. M. Bonmatin, M. Genest, M. C. Petit, E. Gincel, Jean-Pierre Simorre, et al.. Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects.. Biochimie, Elsevier, 1992, 74 (9-10), pp.825-36. ⟨hal-00433186⟩

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