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

2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

316
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...
316
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

338
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...
338
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

1.2K
The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
1.2K
Protein Organization01:24

Protein Organization

7.7K
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....
7.7K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

940
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
940
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

11.7K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
11.7K

You might also read

Related Articles

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

Sort by
Same author

Alpha-synuclein fibrils induce budding of mitochondrial-derived vesicles.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Combining photo-CIDNP and long-lived spin states enables high-contrast detection of weak protein-ligand interactions.

Physical chemistry chemical physics : PCCP·2026
Same author

The NMR Exchange Format (NEF): Specification and Applications.

bioRxiv : the preprint server for biology·2026
Same author

ATP synthase is a promising target for identifying activated and non-activated adipose tissues.

Nature communications·2026
Same author

TNF alpha unmasks enteric malate aspartate shuttle dysfunction bridging Parkinson disease and intestinal inflammation.

Nature communications·2026
Same author

Characterization of flexible RNA binding by tandem RNA recognition motifs through integrative ensemble modelling.

Nucleic acids research·2026
Same journal

pyTRACTnmr: an open source python package for analyzing [<sup>15</sup>N, <sup>1</sup>H]-TRACT experiments.

Journal of biomolecular NMR·2026
Same journal

RelCalc: symbolic evaluation of BWR theory relaxation rates in python, applications to TROSY effects in AX[Formula: see text] spin systems.

Journal of biomolecular NMR·2026
Same journal

Solution NMR study of the titin I-band IgI domain I82 shows unusual conformational dynamics.

Journal of biomolecular NMR·2026
Same journal

Methyl-specific NMR of therapeutic antibodies: cost-effective isotopic labeling strategies in CHO cells for high-resolution structural characterization.

Journal of biomolecular NMR·2026
Same journal

AMIGO - Guided assignment of <sup>13</sup>C-methyl labelled proteins.

Journal of biomolecular NMR·2026
Same journal

Super-Resolution solid-state NMR Spectroscopy.

Journal of biomolecular NMR·2026
See all related articles

Related Experiment Video

Updated: Sep 29, 2025

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

15.6K

Optimization and validation of multi-state NMR protein structures using structural correlations.

Dzmitry Ashkinadze1, Harindranath Kadavath1, Roland Riek2

  • 1Laboratory of Physical Chemistry, ETH Zürich, 8093, Zürich, Switzerland.

Journal of Biomolecular NMR
|March 19, 2022
PubMed
Summary
This summary is machine-generated.

A new method, PDBcor, enhances the analysis of multi-state protein structures determined by liquid-state NMR. This tool quantifies protein state clustering, offering deeper insights into protein dynamics and structure validation.

Keywords:
Multi-state protein structuresProtein structure analysisProtein structure calculationeNOE

More Related Videos

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

9.7K
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

15.6K

Related Experiment Videos

Last Updated: Sep 29, 2025

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

15.6K
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

9.7K
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

15.6K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Liquid-state NMR spectroscopy advances protein structure determination.
  • Elucidating multi-state protein conformations reveals protein dynamics at atomic resolution.
  • Current evaluation methods for NMR-derived multi-state structures include visual inspection, target function values, and RMSD.

Purpose of the Study:

  • To introduce and evaluate PDBcor as a novel measure for multi-state protein structure analysis.
  • To provide an alternative or complementary approach to existing evaluation methods.
  • To demonstrate the utility of PDBcor in various assays for multi-state protein structure calculations.

Main Methods:

  • Utilized a recently introduced structural correlation measure, PDBcor.
  • Applied PDBcor to quantify the clustering of protein states.
  • Demonstrated applications in validating experimental restraints, optimizing state numbers, and analyzing correlation networks.

Main Results:

  • PDBcor quantifies protein state clustering, offering an additional metric for multi-state protein structure analysis.
  • The method is applicable to diverse assays, including validation of distance restraints and NOE network analysis.
  • PDBcor aids in optimizing the number of protein states and estimating their populations.

Conclusions:

  • PDBcor serves as a valuable tool for the quality analysis of multi-state protein structures derived from NMR.
  • It provides quantitative insights into protein dynamics and conformational ensembles.
  • The method enhances the understanding of protein correlation networks and structural ensembles.