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

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...
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,...
Carbon Dioxide Transport in the Blood01:19

Carbon Dioxide Transport in the Blood

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...
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

You might also read

Related Articles

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

Sort by
Same author

Structural insights into a conserved mechanism of choline translocation through CHT.

Science advances·2026
Same author

<i>In Silico</i> Optimization of a Bifunctional Lipase-Polyethylene Terephthalate (PET) Hydrolase for Enhanced PET and Lipid Hydrolysis.

Journal of chemical information and modeling·2026
Same author

Molecular Insights into the Activation of a Fungal Copper Radical Oxidase by Peroxidases.

Chem & bio engineering·2026
Same author

A la carte bioprospecting of substrate-selective laccases via high-throughput computational enzyme-substrate interaction profiling.

Protein science : a publication of the Protein Society·2026
Same author

Engineering <i>Escherichia coli</i> for polyethylene terephthalate powder biodegradation via recoding of an outer membrane protein.

iScience·2026
Same author

Unraveling the impact of cyclic peptide primary structure on rotaxane formation through umbrella sampling molecular dynamics simulations.

Physical chemistry chemical physics : PCCP·2026

Related Experiment Video

Updated: May 24, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

An atomistic view on human hemoglobin carbon monoxide migration processes.

M Fátima Lucas1, Víctor Guallar

  • 1Joint BSC-IRB Research Program in Computational Biology, Barcelona Supercomputing Center, Barcelona, Spain.

Biophysical Journal
|March 6, 2012
PubMed
Summary

Computational methods reveal new insights into how ligands move within hemoglobin. The study shows specific residues influence these ligand diffusion pathways, differing between alpha and beta subunits.

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

Simultaneous Evaluation of Cerebral Hemodynamics and Light Scattering Properties of the In Vivo Rat Brain Using Multispectral Diffuse Reflectance Imaging
07:06

Simultaneous Evaluation of Cerebral Hemodynamics and Light Scattering Properties of the In Vivo Rat Brain Using Multispectral Diffuse Reflectance Imaging

Published on: May 7, 2017

Related Experiment Videos

Last Updated: May 24, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Simultaneous Evaluation of Cerebral Hemodynamics and Light Scattering Properties of the In Vivo Rat Brain Using Multispectral Diffuse Reflectance Imaging
07:06

Simultaneous Evaluation of Cerebral Hemodynamics and Light Scattering Properties of the In Vivo Rat Brain Using Multispectral Diffuse Reflectance Imaging

Published on: May 7, 2017

Area of Science:

  • Biophysics
  • Computational Chemistry
  • Molecular Biology

Background:

  • Human hemoglobin's atomistic mechanism is extensively studied, yet ligand diffusion remains poorly understood.
  • Existing research presents conflicting theories on ligand migration pathways within hemoglobin.

Purpose of the Study:

  • To investigate ligand diffusion mechanisms in human hemoglobin using advanced computational techniques.
  • To elucidate the role of specific amino acid residues and tertiary structure in ligand dynamics.

Main Methods:

  • Utilized the PELE (Program for Electronic-Like Energy) computational method for simulating ligand migration.
  • Validated the methodology by comparing results of carbon monoxide (CO) migration in myoglobin with existing theoretical and experimental data.
  • Analyzed ligand diffusion in both tense and relaxed states of hemoglobin, differentiating between alpha and beta subunits.

Main Results:

  • The proximal site (hemoglobin's Xe1 cavity equivalent) is not a visited site during ligand migration.
  • Strategically located residues were identified as key modulators of ligand diffusion within hemoglobin subunits.
  • Multiple, diversified diffusion pathways were observed, particularly within the alpha-globin subunits.
  • Ligand dynamics demonstrated a significant dependence on the protein's tertiary structure.

Conclusions:

  • The PELE method provides a robust approach to study controversial ligand migration processes in hemoglobin.
  • Specific amino acid residues and the tertiary structure play critical roles in dictating ligand diffusion pathways.
  • Understanding these dynamics offers new perspectives on hemoglobin function and potential therapeutic targets.