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Structural determinants of salmon calcitonin bioactivity: the role of the Leu-based amphipathic alpha-helix.
Andreotti G, Méndez BL, Amodeo P, Morelli MA, Nakamuta H, Motta A. Andreotti G, et al. Among authors: amodeo p. J Biol Chem. 2006 Aug 25;281(34):24193-203. doi: 10.1074/jbc.M603528200. Epub 2006 Jun 9. J Biol Chem. 2006. PMID: 16766525 Free article.
Salmon calcitonin (sCT) forms an amphipathic helix in the region 9-19, with the C-terminal decapeptide interacting with the helix (Amodeo, P., Motta, A., Strazzullo, G., Castiglione Morelli, M. A. (1999) J. ...
Salmon calcitonin (sCT) forms an amphipathic helix in the region 9-19, with the C-terminal decapeptide interacting with the helix (Amodeo …
SDS-resistant active and thermostable dimers are obtained from the dissociation of homotetrameric beta-glycosidase from hyperthermophilic Sulfolobus solfataricus in SDS. Stabilizing role of the A-C intermonomeric interface.
Gentile F, Amodeo P, Febbraio F, Picaro F, Motta A, Formisano S, Nucci R. Gentile F, et al. Among authors: amodeo p. J Biol Chem. 2002 Nov 15;277(46):44050-60. doi: 10.1074/jbc.M206761200. Epub 2002 Sep 3. J Biol Chem. 2002. PMID: 12213823 Free article.
106 results