High-resolution 1H-NMR studies of monomeric melittin in aqueous solution - PubMed (original) (raw)
Comparative Study
High-resolution 1H-NMR studies of monomeric melittin in aqueous solution
J Lauterwein et al. Biochim Biophys Acta. 1980.
Abstract
High resolution 1H-NMR at 360 MHz was used to characterize monomeric melittin in aqueous solution. The monomeric form of melittin was found to prevail at 3 mM concentration, pH 3.0, and temperatures between 30 and 90 degrees C, both in the absence of salt and with 6 M guanidium chloride. From comparison with model peptides and studies of the effects of 6 M guanidium chloride and variable temperature on the NMR parameters it was concluded that monomeric melittin is predominantly in an extended flexible form, with the fragments 5--9 and 14--20 more highly structured than the rest of the amino acid sequence. The appearance of a second, low abundant form of monomeric melittin, which is in slow exchange on the NMR time scale with both the more abundant monomeric conformation and aggregated melittin, was attributed to cis-trans isomerism of the peptide bond Leu-13--Pro-14.
Similar articles
- High-resolution 1H-NMR studies of self-aggregation of melittin in aqueous solution.
Brown LR, Lauterwein J, Wüthrich K. Brown LR, et al. Biochim Biophys Acta. 1980 Apr 25;622(2):231-44. doi: 10.1016/0005-2795(80)90034-3. Biochim Biophys Acta. 1980. PMID: 7378452 - Physicochemical studies of the protein-lipid interactions in melittin-containing micelles.
Lauterwein J, Bösch C, Brown LR, Wüthrich K. Lauterwein J, et al. Biochim Biophys Acta. 1979 Sep 21;556(2):244-64. doi: 10.1016/0005-2736(79)90046-4. Biochim Biophys Acta. 1979. PMID: 534626 - High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface.
Brown LR, Braun W, Kumar A, Wüthrich K. Brown LR, et al. Biophys J. 1982 Jan;37(1):319-28. doi: 10.1016/S0006-3495(82)84680-8. Biophys J. 1982. PMID: 6275926 Free PMC article. - The actions of melittin on membranes.
Dempsey CE. Dempsey CE. Biochim Biophys Acta. 1990 May 7;1031(2):143-61. doi: 10.1016/0304-4157(90)90006-x. Biochim Biophys Acta. 1990. PMID: 2187536 Review. - Melittin, the Major Pain-Producing Substance of Bee Venom.
Chen J, Guan SM, Sun W, Fu H. Chen J, et al. Neurosci Bull. 2016 Jun;32(3):265-72. doi: 10.1007/s12264-016-0024-y. Epub 2016 Mar 17. Neurosci Bull. 2016. PMID: 26983715 Free PMC article. Review.
Cited by
- The effect of counterions on melittin aggregation.
Tatham AS, Hider RC, Drake AF. Tatham AS, et al. Biochem J. 1983 Jun 1;211(3):683-6. doi: 10.1042/bj2110683. Biochem J. 1983. PMID: 6882364 Free PMC article. - 13C alpha-NMR assignments of melittin in methanol and chemical shift correlations with secondary structure.
Buckley P, Edison AS, Kemple MD, Prendergast FG. Buckley P, et al. J Biomol NMR. 1993 Nov;3(6):639-52. doi: 10.1007/BF00198369. J Biomol NMR. 1993. PMID: 8111230 - Conformational sampling of peptides in cellular environments.
Tanizaki S, Clifford J, Connelly BD, Feig M. Tanizaki S, et al. Biophys J. 2008 Feb 1;94(3):747-59. doi: 10.1529/biophysj.107.116236. Epub 2007 Sep 28. Biophys J. 2008. PMID: 17905846 Free PMC article. - Nuclear Magnetic Resonance-Based Structural Characterization and Backbone Dynamics of Recombinant Bee Venom Melittin.
Ramirez L, Shekhtman A, Pande J. Ramirez L, et al. Biochemistry. 2018 May 15;57(19):2775-2785. doi: 10.1021/acs.biochem.8b00156. Epub 2018 Apr 30. Biochemistry. 2018. PMID: 29668274 Free PMC article. - Effect of pressure on the self-association of melittin.
Thompson RB, Lakowicz JR. Thompson RB, et al. Biochemistry. 1984 Jul 17;23(15):3411-7. doi: 10.1021/bi00310a005. Biochemistry. 1984. PMID: 6466646 Free PMC article.