Solution structure of μ-conotoxin GIIIA analysed by 2D-NMR and distance geometry calculations

• Published in: FEBS letters Vol. 278; no. 2; pp. 160 - 166
• Main Authors: Ott, Karl Heinz, Becker, Stefan, Gordon, Robert D., Rüterjans, Heinz
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 28.01.1991; Elsevier
• Subjects: 2-dimensional (2D) nuclear-Overhauser-enhancement spectroscopy; 4 trans-hydroxy-L-proline; 4-methoxy-2,3,6-trimethyl-benzenesulphonyl; Amino Acid Sequence; Aminoacids, peptides. Hormones. Neuropeptides; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Canus geographus; Computer Graphics; Conotoxins; dAN; distance between Hα(i) and HN(i); distance between Hα(i) and HN(i+1); Distance geometry; dNA; dNB, dBN, dNN; double quantum filtered correlated spectroscopy; DQf COSY; E. COSY; exclusive COSY; Fundamental and applied biological sciences. Psychology; Geographutoxin; high pressure liquid chromatography; HLPC; Hyp; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Mtr; Neurotoxins - chemistry; NMR; NMR, 2D; NOE; NOESY; nuclear magnetic resonance; nuclear Overhauser enhancement; Peptide synthesis; Peptides, Cyclic - chemistry; Protein Conformation; Proteins; ROESY; rotating frame Overhauser enhancement spectroscopy; similar for Hβ and HN; Snails; Solutions; TOCSY; total correlated spectroscopy; μ-Conotoxin GIIIA; μ-Conotoxin GIIIA; DQf COSY; Geographutoxin; Distance geometry; NOE; ROESY; E. COSY; Canus geographus; TOCSY; Mtr; dAN; NMR; dNB, dBN, dNN; dNA; HLPC; NMR, 2D; Peptide synthesis; NOESY; Hyp; Chemical shift; Peptides; Neurotoxin; NMR spectrometry; Stereochemistry; Spatial structure; Computer aid; Aminoacid sequence; Conformation; Two dimension spectrometry
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(91)80107-E

We have investigated the structure of μ-conotoxin GIIIA by 2D-NMR methods. The assignment of 1H NMR spectra and a quantitative analysis of NOE and J-coupling data are presented. These results were used for the calculation of secondary structure elements of μ-conotoxin GIIIA. Distance geometry calculations were carried out to define the global folding of the peptide.