Related Experiment Video
Updated: Jun 25, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Asymmetry in 13C-13C COSY spectra provides information on ligand geometry in paramagnetic proteins
Ivano Bertini1, Beatriz Jiménez, Mario Piccioli
1Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy. ivanobertini@cerm.unifi.it
Abstract:
The relative intensity of Calpha-C' cross-peaks in homonuclear 13C COSY spectra depends on the relaxation properties of Calpha and C' spins, which, in the proximity of a paramagnetic center, are related to the metal-to-carbon distance. Their quantitative analysis has lead, for the cerium-substituted dicalcium protein, calbindin D9k, to the straightforward identification of peaks arising from metal-coordinating groups. The monodentate or bidentate metal binding mode of carboxylates was identified directly via NMR.
More Related Videos
12:47Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
14:55Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Related Concept Videos
¹H NMR: Interpreting Distorted and Overlapping Signals
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...
Carbon-13 (¹³C) NMR: Overview
2D NMR: Homonuclear Correlation Spectroscopy (COSY)
NMR Spectroscopy: Spin–Spin Coupling
¹³C NMR: ¹H–¹³C Decoupling
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
2D NMR: Overview of Homonuclear Correlation Techniques
COSY90 is the standard two-dimensional (2D) COSY experiment that...