Related Experiment Video
Updated: Oct 8, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
Published on: April 19, 2021
A 2D NMR study of the internal flexibility of the antifungal peptide stendomycin
J P Simorre1, D Genest, A Caille
1CBM-CNRS, Orléans, France.
Abstract:
A 2-D 1H NMR study (NOESY, COSY, HOHAHA and ROESY experiments) of the antifungal peptide stendomycin is presented. The variation of the NOESY cross peak intensities is measured as a function of temperature in order to discriminate between constant and fluctuating interproton distances. It is shown that among 71 NOESY cross peaks, only 12 correspond to well defined interproton distances and their correlation time is determined. The other cross peaks cannot be translated accurately in terms of distances owing to internal molecular motions. (1H)-13C nOe measurements confirm the internal mobility of the molecule. Finally a flexibility map of stendomycin can be established.
More Related Videos
Related Concept Videos
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
NMR Spectroscopy: Spin–Spin Coupling
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
NMR Spectroscopy Of Amines
Antifungal Agents

