Structure of Apamin in Solution: A Two-Dimensional Nuclear Magnetic Resonance Study

David Wemmer, Neville R. Kallenbach

Research output: Contribution to journalArticlepeer-review

Abstract

A two-dimensional (2-D) Fourier-transform nuclear magnetic resonance (NMR) study of the 18 amino acid neurotoxin apamin isolated from honeybee venom is reported. Combining 2-D J-correlated spectra with 2-D nuclear Overhauser spectra in H2O solution permits essentially complete assignment of the 1H NMR spectrum of apamin at a fixed pH, including a number of spin systems that are reported for the first time. The structural model previously derived by Bystrov et al. [Bystrov, V. F., Okhanov, V. V., Miroshnikov, A. I., & Ovchinnikov, Yu. A. (1980) FEBS Lett. 119, 113–116] from NMR data is shown to be largely correct. The 2-D nuclear Overhauser effect (NOE) spectrum in particular reveals a series of amide-amide NOE's consistent with an α-helical core (residues 9–15) in the molecule. NOE's between amide and Cα protons, followed by amide to amide NOE's, indicate a β-turn involving residues 3–5 and a nonstandard turn including residues 6–8. We find no evidence for the β-type structure postulated at the C terminus, however. Instead, it appears that the α-helix continues with increasing fraying from residues 16–18.

Original languageEnglish (US)
Pages (from-to)1901-1906
Number of pages6
JournalBiochemistry
Volume22
Issue number8
DOIs
StatePublished - 1983

ASJC Scopus subject areas

  • Biochemistry

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