Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

1.7K
The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse....
1.7K
Protein Organization01:24

Protein Organization

9.9K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
9.9K
Protein Folding01:22

Protein Folding

129.9K
Overview
129.9K
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

769
Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
769
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

872
Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other...
872

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Controlled Dimerization of Rhodium(I) Isocyanides Enables Photophysical Properties Beyond Mononuclear Complexes.

JACS Au·2026
Same author

Non-Dilute Synthesis of Macrodiolides and Macrotetrolides Enabled by Confinement Catalysis.

Angewandte Chemie (International ed. in English)·2026
Same author

TASP1-mediated cleavage of REV3L enhances the activity of DNA polymerase ζ in mammalian cells.

Nature communications·2026
Same author

NMR detects clustering and ultra-weak excipient interactions governing monoclonal antibody viscosity in formulation-relevant conditions.

mAbs·2026
Same author

Photoactive four-coordinate copper(I) complexes based on chelating diimine, diphosphine, and diisocyanide ligands with high excited-state energies.

Dalton transactions (Cambridge, England : 2003)·2026
Same author

Advanced NMR Characterization and Sensitive Detection of Isoaspartate in Proteins.

Analytical chemistry·2026
Same journal

Real-Time Vibrational Spectroscopy Reveals an Inversion Transition State in the Photoisomerization of Phenylazoimidazole.

The journal of physical chemistry letters·2026
Same journal

Precursor-Directed Self-Assembly in Hydrothermal Carbon Nitride Nanostructures Revealed by Nano-FTIR.

The journal of physical chemistry letters·2026
Same journal

Correction to "Equation-of-Motion Block-Correlated Coupled Cluster Method for Excited Electronic States of Strongly Correlated Systems".

The journal of physical chemistry letters·2026
Same journal

Rationalizing Stacking-Dependent Charge Injection Dynamics in Radical-Based Organic Light-Emitting Diodes.

The journal of physical chemistry letters·2026
Same journal

Bottom-Up Formation of the Simplest Geminal Thiol─Methanedithiol (CH<sub>2</sub>(SH)<sub>2</sub>)─and the Methyl Hydrodisulfide (H<sub>3</sub>CSSH) Isomer in Interstellar Analogue Ices.

The journal of physical chemistry letters·2026
Same journal

Trion Mediated Sequential Charge Separation in Functionalized CsPbBr<sub>3</sub>/AgInS<sub>2</sub> Hybrid Nanocrystals.

The journal of physical chemistry letters·2026
See all related articles

Related Experiment Video

Updated: Mar 18, 2026

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.9K

In-Cell Protein Structures from 2D NMR Experiments.

Thomas Müntener1, Daniel Häussinger1, Philipp Selenko2

  • 1Department of Chemistry, University of Basel , St. Johanns-Ring 19, 4056 Basel, Switzerland.

The Journal of Physical Chemistry Letters
|July 6, 2016
PubMed
Summary
This summary is machine-generated.

We developed a new method using paramagnetic lanthanide tags for in-cell NMR to determine protein structures within cells. This technique provides atomic-level detail for protein structure determination in living cells.

More Related Videos

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

16.1K
Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor
10:25

Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor

Published on: March 9, 2021

3.9K

Related Experiment Videos

Last Updated: Mar 18, 2026

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.9K
Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

16.1K
Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor
10:25

Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor

Published on: March 9, 2021

3.9K

Area of Science:

  • Structural Biology
  • Biophysics
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • In-cell NMR spectroscopy offers atomic resolution insights into protein structures within living cells.
  • However, its application for *de novo* protein structure determination is limited.
  • Existing methods often require high protein concentrations or specialized equipment.

Purpose of the Study:

  • To introduce a novel paramagnetic lanthanide-tagging approach for in-cell NMR.
  • To enable simultaneous measurement of protein pseudocontact shifts (PCSs) and residual dipolar couplings (RDCs).
  • To facilitate *de novo* protein structure determination within intact cells.

Main Methods:

  • Utilized a paramagnetic lanthanide-tag to generate PCSs and RDCs.
  • Integrated PCS and RDC data into Rosetta structure calculation software.
  • Performed 2D in-cell NMR experiments on Xenopus laevis oocytes.
  • Analyzed low-concentration (∼50 μM) samples at moderate magnetic field strengths (600 MHz).

Main Results:

  • Successfully determined the structure of the protein G B1 domain (GB1) in intact Xenopus laevis oocytes.
  • Derived well-defined GB1 ensembles from the in-cell NMR data.
  • Demonstrated the feasibility of structure determination from a single set of 2D experiments.

Conclusions:

  • The paramagnetic lanthanide-tagging method is an effective tool for in-cell protein structure determination.
  • This approach provides an accessible alternative for studying intracellular protein structures.
  • Enables atomic-resolution structural insights directly within the cellular environment.