Related Experiment Video
Updated: Aug 15, 2026

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE
Published on: May 16, 2017
High-resolution 1H NMR study of the solution structure of delta-hemolysin
M J Tappin1, A Pastore, R S Norton
1Department of Biochemistry, University of Oxford, U.K.
Abstract:
The 26-residue toxin from Staphylococcus aureus, delta-hemolysin, is thought to act by traversing the plasma membrane. The structure of this peptide, in methanol solution, has been investigated by using high-resolution NMR in combination with molecular dynamics calculations. The 1H NMR spectrum has been completely assigned, and it is shown that residues 2-20 form a relatively stable helix while the residues at the C-terminal end appear to be more flexible. The structures were calculated only from nuclear Overhauser effect data and standard bond lengths. It is shown that the results are consistent with 3JNH-alpha CH coupling constants and amide hydrogen exchange rates.
More Related Videos
Related Concept Videos
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
¹H NMR of Labile Protons: Temporal Resolution
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
¹H NMR of Labile Protons: Deuterium (²H) Substitution
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

