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

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

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

1.3K
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...
1.3K
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

5.8K
Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
5.8K

You might also read

Related Articles

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

Sort by
Same author

QproMS: a web application for label-free proteomic data analysis.

Bioinformatics advances·2026
Same author

Integrative structural analysis of the human LRP2-LRPAP1 complex reveals multiple regulatory sites.

Communications biology·2026
Same author

Molecular recognition of thyroglobulin by sortilin.

Nature communications·2026
Same author

IHMValidation: Assessment of Integrative Structure Models Deposited to the Protein Data Bank.

Journal of molecular biology·2025
Same author

Structure and assembly of the A-C linker connecting microtubule triplets in centrioles.

Science advances·2025
Same author

Breaking Boundaries in Histone Modification MS-Based Detection: A Tailored Search Strategy for Unrestricted Identification of Novel Epigenetic Marks.

Molecular & cellular proteomics : MCP·2025

Related Experiment Video

Updated: May 6, 2026

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
07:11

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

6.9K

IHMCIF: An Extension of the PDBx/mmCIF Data Standard for Integrative Structure Determination Methods.

Brinda Vallat1, Benjamin M Webb2, John D Westbrook1

  • 1Research Collaboratory for Structural Bioinformatics Protein Data Bank and the Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA; Cancer Institute of New Jersey, Rutgers, The State University of New Jersey, New Brunswick, NJ 08901, USA.

Journal of Molecular Biology
|March 20, 2024
PubMed
Summary

The Integrative and Hybrid Methods Chemical Information File (IHMCIF) framework aids in archiving and sharing macromolecular structures from integrative modeling. This advancement supports FAIR data principles for structural biology research.

Keywords:
Data StandardIHMCIFPDB-DevPDBx/mmCIFWorldwide Protein Data Bank

More Related Videos

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

6.4K
Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening
14:04

Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening

Published on: January 16, 2021

4.7K

Related Experiment Videos

Last Updated: May 6, 2026

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
07:11

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

6.9K
Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

6.4K
Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening
14:04

Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening

Published on: January 16, 2021

4.7K

Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Biology

Background:

  • The Protein Data Bank (PDB) archives experimentally determined macromolecular structures.
  • Integrative or Hybrid Modeling (IHM) generates structural models spanning multiple scales and states.
  • Existing frameworks like PDBx/mmCIF are primarily for experimentally determined atomic structures.

Purpose of the Study:

  • To introduce IHMCIF, a data information framework for archiving and disseminating macromolecular structures derived from IHM.
  • To extend the PDBx/mmCIF standard to accommodate the complexities of integrative structural biology.
  • To establish a foundational data standard for the PDB-Dev prototype system.

Main Methods:

  • IHMCIF is developed as an extension of the PDBx/mmCIF framework.
  • It incorporates flexible data representation to describe integrative structures.
  • Definitions for restraints from diverse experimental methods are included.

Main Results:

  • IHMCIF supports the archiving and dissemination of IHM-derived structures.
  • It provides a flexible data model for complex biological assemblies.
  • The framework was developed with significant community input.

Conclusions:

  • IHMCIF facilitates the FAIR data principles for integrative structural biology.
  • It serves as the data standard for the PDB-Dev system.
  • Ultimately, IHMCIF will enable the integration of PDB-Dev data into the main PDB archive.