Related Experiment Video

Updated: Jul 31, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Determination of glycopeptide primary structure by 360-MHz proton magnetic resonance spectroscopy

J P Carver, A A Grey

    Biochemistry
    |November 10, 1981
    PubMed

    More Related Videos

    Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics09:09

    Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics

    Published on: October 13, 2020

    Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue07:40

    Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

    Published on: May 17, 2024

    Related Concept Videos

    Proton (¹H) NMR: Chemical Shift01:07

    Proton (¹H) NMR: Chemical Shift

    Organic molecules primarily contain carbon and hydrogen atoms. While all the hydrogen isotopes are NMR-active, protium or hydrogen-1 is the most abundant. It has a significant energy separation between its nuclear spin states due to its large gyromagnetic ratio. As per Boltzmann's distribution, an increase in the energy separation implies a greater excess population of nuclei available for excitation, resulting in a strong NMR absorption signal.
    Absorption signals of all the protium nuclei in a...
    ¹H NMR: Complex Splitting01:13

    ¹H NMR: Complex Splitting

    A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
    Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied first.
    ¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

    ¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

    When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
    NMR Spectroscopy and Mass Spectrometry of Aldehydes and Ketones01:15

    NMR Spectroscopy and Mass Spectrometry of Aldehydes and Ketones

    In aldehydes, the hydrogen atom connected to the carbonyl carbon helps distinguish aldehydes from other carbonyl compounds using ¹H NMR spectroscopy. The closeness of aldehydic hydrogen to the electrophilic carbonyl carbon highly deshields the hydrogen atom causing its signal to appear around 10 ppm in the ¹H NMR spectra. α hydrogens split the aldehydic proton signal, which helps identify the number of α hydrogens in the molecule. For instance, one α hydrogen creates a doublet for an aldehydic...
    NMR and Mass Spectroscopy of Carboxylic Acids01:30

    NMR and Mass Spectroscopy of Carboxylic Acids

    In ¹H NMR spectroscopy, acidic protons (–COOH) of carboxylic acids are highly deshielded and absorb far downfield, at around 9–12 ppm. The chemical shift value depends on the concentration and solvent used.
    While α protons of carboxylic acids absorb at 2–2.5 ppm, β protons absorb further upfield.
    Carboxylic acids are easily identified by dissolving them in deuterium oxide, which results in a rapid exchange of the acidic protons with deuterium. This leads to the disappearance of the acidic...
    Peptide Identification Using Tandem Mass Spectrometry01:33

    Peptide Identification Using Tandem Mass Spectrometry

    Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
    This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...