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

Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
Hemoglobin01:24

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Respiration and Gaseous Exchange01:20

Respiration and Gaseous Exchange

The intricate interplay between the cardiovascular and respiratory systems is crucial for efficiently transporting respiratory gases throughout the body. Let us explore the cardiovascular system's multifaceted functions, emphasizing its pivotal role in gas exchange.
Respiration involves the exchange of gases, especially oxygen (O2) and carbon dioxide (CO2), between the alveoli and body cells, a process facilitated by blood circulation. As a result, the cardiovascular system, which involves the...
Gas Exchange and Transport01:20

Gas Exchange and Transport

Gas exchange, the intake of molecular oxygen (O2) from the environment and the outflow of carbon dioxide (CO2) into the environment, is necessary for cellular function. Gas exchange during respiration occurs largely via the movement of gas molecules along pressure gradients. Gas travels from areas of higher partial pressure to areas of lower partial pressure. In mammals, gas exchange occurs in the alveoli of the lungs, which are adjacent to capillaries and share a membrane with them.
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Respiration Pathways01:26

Respiration Pathways

Cellular respiration is a fundamental metabolic process that enables organisms to generate energy from organic molecules. One of its central pathways is the tricarboxylic acid (TCA) cycle, also known as the Krebs cycle, which plays a crucial role in energy production and biosynthetic processes.Conversion of Pyruvate to Acetyl-CoAThe pyruvate generated from glycolysis undergoes oxidative decarboxylation by the pyruvate dehydrogenase complex, producing acetyl-CoA, one molecule of NADH, and one...

You might also read

Related Articles

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

Sort by
Same author

On the Bona Fide Sampling of Reaction Candidates in Red Moon Method by Replica-Exchange Molecular Dynamics Method: REMD-RM Method and Its Efficacy in Polymerization and Cross-Linking Reactions of Polypropylene.

Journal of computational chemistry·2026
Same author

Atomistic Simulation of Ion Pair Aggregates of a (Pyridylamido)Hf(IV) Catalyst: Energetic Destabilization and Structural Diversity Induced by Monomer, Chain Transfer Agent, and Growing Polymer Chain.

The journal of physical chemistry. B·2026
Same author

Ready-to-Use Polymerization Simulations Combining Universal Machine Learning Interatomic Potential with Time-Dependent Bond Boosting for Polymer and Interface Design.

The journal of physical chemistry. B·2026
Same author

Blind prediction of complex water and ion ensembles around RNA in CASP16.

bioRxiv : the preprint server for biology·2025
Same author

Blind Prediction of Complex Water and Ion Ensembles Around RNA in CASP16.

Proteins·2025
Same author

Atomistic simulation of olefin polymerization reaction by organometallic catalyst: significant role of microscopic structural dynamics of (pyridylamido) Hf(IV) complex in catalytic reactivity.

Frontiers in chemistry·2025

Related Experiment Video

Updated: May 12, 2026

Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions
10:40

Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions

Published on: December 28, 2016

Oxygen entry through multiple pathways in T-state human hemoglobin.

Masayoshi Takayanagi1, Ikuo Kurisaki, Masataka Nagaoka

  • 1Venture Business Laboratory, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.

The Journal of Physical Chemistry. B
|April 26, 2013
PubMed
Summary

Researchers mapped oxygen (O2) entry pathways into human hemoglobin (HbA) using molecular dynamics simulations. This study reveals multiple O2 entry routes, aiding understanding of hemoglobin

More Related Videos

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Related Experiment Videos

Last Updated: May 12, 2026

Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions
10:40

Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions

Published on: December 28, 2016

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Area of Science:

  • Biophysics
  • Computational Biology
  • Structural Biology

Background:

  • The oxygen (O2) binding site in human hemoglobin (HbA) is internal, leading to questions about O2 access.
  • Understanding O2 entry mechanisms is crucial for comprehending hemoglobin's function.

Purpose of the Study:

  • To identify and characterize all significant O2 entry pathways into the T-state tetramer HbA from the solvent.
  • To visualize the shape and relative importance of these identified O2 entry pathways.

Main Methods:

  • Utilized ensemble molecular dynamics (MD) simulations with 128 independent 8 ns trajectories.
  • Simulated O2 entry processes in an O2-rich aqueous solvent.
  • Developed an intrinsic pathway identification by clustering method.

Main Results:

  • Detected 141 and 425 O2 entry events in the α and β subunits of HbA, respectively.
  • Visualized multiple O2 entry pathways, detailing their shapes and relative significance.
  • Estimated O2 entry rate constants consistent with experimental observations.

Conclusions:

  • O2 molecules access the HbA binding site through multiple distinct pathways.
  • The developed pathway mapping provides a foundation for future atomic-level analyses of HbA O2 binding.
  • Findings support a multi-pathway model for O2 diffusion into hemoglobin.