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

Carbon-dioxide Fixation01:28

Carbon-dioxide Fixation

875
Carbon dioxide fixation in prokaryotes enables the assimilation of inorganic carbon into organic molecules, supporting biosynthetic pathways, sustaining ecosystems, and contributing to the global carbon cycle. It also has industrial applications in carbon capture and bioproduct synthesis. Autotrophic organisms rely on this process to utilize CO₂ as a carbon source in diverse environments.The Calvin CycleThe Calvin cycle is the most widespread carbon fixation mechanism, primarily used by...
875
Carbon Dioxide Transport in the Blood01:19

Carbon Dioxide Transport in the Blood

6.9K
Carbon dioxide (CO2) transport in the blood is critical to human physiology. On average, our body cells produce around 200 mL of CO2 per minute, precisely the quantity expelled by the lungs. This process involves the transportation of CO2 from the tissue cells to the lungs in three primary forms.
Forms of CO2 Transport
1. Dissolved in plasma: A small percentage (7-10%) of CO2 is transported and dissolved directly in the plasma.
2. Carbaminohemoglobin: Just over 20% of CO2 is chemically bound to...
6.9K
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

6.2K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
6.2K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

13.7K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
13.7K
Protein Transport to the Thylakoids01:22

Protein Transport to the Thylakoids

3.1K
Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
3.1K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.9K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
6.9K

You might also read

Related Articles

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

Sort by
Same author

New Docking, Molecular Dynamics, and QSAR Models to Predict Disruption of Human and Rat Transthyretin Function by Per- and Polyfluoroalkyl Substances (PFAS).

Chemical research in toxicology·2026
Same author

Defining the Mechanism of Action and Resistance of New <i>Mycobacterium abscessus</i> MmpL3 Inhibitors.

ACS chemical biology·2026
Same author

Nitrile RC≡N Triple Bond Cleavage by a Dicopper Nitrite Complex with N<sub>2</sub> Elimination and Formation of RCO<sub>2</sub><sup>-</sup> Carboxylate Ligands.

Journal of the American Chemical Society·2026
Same author

Bioaccumulation of PFOS Isomers in Transporter Proteins.

Chemical research in toxicology·2026
Same author

Thermochemical properties of small rhenium molecules: ReC, ReN, ReO, ReS, and ReC2.

The Journal of chemical physics·2025
Same author

Perspective on Many-Body Methods for Molecular Polaritonic Systems.

Journal of chemical theory and computation·2025

Related Experiment Video

Updated: Apr 5, 2026

Metabolic Pathway Confirmation and Discovery Through 13C-labeling of Proteinogenic Amino Acids
07:26

Metabolic Pathway Confirmation and Discovery Through 13C-labeling of Proteinogenic Amino Acids

Published on: January 26, 2012

25.2K

Carbon Dioxide Migration Pathways in Proteins.

Michael L Drummond1, Angela K Wilson1, Thomas R Cundari1

  • 1Center for Advanced Scientific Computing and Modeling (CASCaM), Department of Chemistry, University of North Texas, Denton, Texas 76203-5070, United States.

The Journal of Physical Chemistry Letters
|August 20, 2015
PubMed
Summary
This summary is machine-generated.

Researchers mapped carbon dioxide (CO2) movement within the phosphoenolpyruvate carboxykinase enzyme. Molecular dynamics simulations revealed three distinct pathways, indicating the enzyme actively guides CO2, with implications for biotechnology.

Keywords:
carbon capture and sequestrationligand migrationmolecular dynamicsphosphoenolpyruvate carboxykinaseprotein−ligand interactions

More Related Videos

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.6K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.8K

Related Experiment Videos

Last Updated: Apr 5, 2026

Metabolic Pathway Confirmation and Discovery Through 13C-labeling of Proteinogenic Amino Acids
07:26

Metabolic Pathway Confirmation and Discovery Through 13C-labeling of Proteinogenic Amino Acids

Published on: January 26, 2012

25.2K
Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.6K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.8K

Area of Science:

  • Biochemistry and Molecular Biology
  • Enzymology
  • Biophysics

Background:

  • Protein-gas interactions are crucial for fundamental biological processes like carbon fixation.
  • Understanding molecular mechanisms of enzyme-substrate interactions is key to biological catalysis.

Purpose of the Study:

  • To investigate the migration pathways of carbon dioxide (CO2) within the enzyme phosphoenolpyruvate carboxykinase (PEPCK).
  • To elucidate how protein structure influences CO2 transport at the molecular level.

Main Methods:

  • Utilized extensive all-atom molecular dynamics (MD) simulations.
  • Analyzed simulated trajectories to identify and characterize CO2 diffusion pathways within the enzyme's active site.

Main Results:

  • Identified three discrete migration pathways for CO2 within PEPCK.
  • Demonstrated that the protein actively directs the movement of CO2 through specific channels.
  • Characterized the chemical properties of these identified pathways.

Conclusions:

  • The enzyme PEPCK possesses specific internal pathways that facilitate CO2 transport.
  • These findings highlight the role of protein architecture in guiding substrate motion.
  • The identified pathways offer potential targets for enzyme engineering and biotechnological applications.