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

Multiple Allele Traits01:49

Multiple Allele Traits

37.7K
The Concept of Multiple Allelism
37.7K
Hemoglobin01:24

Hemoglobin

7.0K
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...
7.0K
Protein Complex Assembly02:41

Protein Complex Assembly

16.4K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.4K
Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

5.4K
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,...
5.4K
Protein and Protein Structure02:15

Protein and Protein Structure

86.1K
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...
86.1K
Multipotency of Hematopoietic Stem Cells01:19

Multipotency of Hematopoietic Stem Cells

3.7K
The hematopoietic stem cells or HSCs are multipotent, meaning they can differentiate and give rise to all blood and immune cells. HSCs are maintained in the quiescent stage until an external stimulus initiates their differentiation. The multipotent HSCs exist as two heterogeneous populations, long-term repopulating cells (LTRC) and short-term repopulating cells (STRC). The two HSC populations have different surface markers or receptors and are classified based on quiescence and long-term...
3.7K

You might also read

Related Articles

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

Sort by
Same author

Mass Spectrometry-Based Characterization and Functional Evaluation of Paralytic Peptides From Bracon brevicornis Venom.

Chemistry, an Asian journal·2026
Same author

From thresholds to trajectories: a perspective on reframing alloimmune risk for computational modeling in solid organ transplantation.

Frontiers in immunology·2026
Same author

Luminescent heparin-functionalized carbon dots with potential applications in nanoparticle-protein interactions and cell imaging.

Scientific reports·2026
Same author

Zoledronic Acid in the Management of Melorheostosis of Radius and Ulna - A Rare Case Report with Literature Review.

Journal of orthopaedic case reports·2026
Same author

Direct Heteronucleation-Enabled Formation of Epitaxial Plasmonic CsPbBr<sub>3</sub>-Cu<sub>2-x</sub>Se Nanocrystal Heterostructures.

Nano letters·2026
Same author

Accelerated amyloid neurodegeneration in HIV-1-infected APP-KI Alzheimer's disease mice.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Dec 26, 2025

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy
07:24

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy

1.9K

Sickle Cell Hemoglobin.

Amit Kumar Mandal1, Amrita Mitra2, Rajdeep Das2

  • 1Department of Biological Sciences, Indian Institute of Science Education and Research Kolkata, Mohanpur, 741246, Nadia, West Bengal, India. amitkm@iiserkol.ac.in.

Sub-Cellular Biochemistry
|March 20, 2020
PubMed
Summary
This summary is machine-generated.

Sickle cell hemoglobin polymerization, the cause of sickle cell anemia, can be inhibited by its oxy form and glutathionylated deoxy form. Elevating glutathionylation may offer a novel therapeutic strategy for sickle cell disease.

Keywords:
Glutathionyl sickle hemoglobinHydrogen/deuterium exchange mass spectrometryOxygen dissociation curvePolymerizationSickle cell anemiaSickle cell hemoglobin

More Related Videos

Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry
08:23

Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry

Published on: November 5, 2019

10.3K
Continuous Manual Exchange Transfusion for Patients with Sickle Cell Disease: An Efficient Method to Avoid Iron Overload
05:23

Continuous Manual Exchange Transfusion for Patients with Sickle Cell Disease: An Efficient Method to Avoid Iron Overload

Published on: March 14, 2017

20.2K

Related Experiment Videos

Last Updated: Dec 26, 2025

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy
07:24

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy

1.9K
Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry
08:23

Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry

Published on: November 5, 2019

10.3K
Continuous Manual Exchange Transfusion for Patients with Sickle Cell Disease: An Efficient Method to Avoid Iron Overload
05:23

Continuous Manual Exchange Transfusion for Patients with Sickle Cell Disease: An Efficient Method to Avoid Iron Overload

Published on: March 14, 2017

20.2K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Sickle cell hemoglobin (HbS) causes sickle cell anemia due to a point mutation leading to βVal6 substitution.
  • Deoxygenated HbS forms polymers via noncovalent interactions, causing sickle-shaped red blood cells (RBCs).
  • Despite understanding the molecular basis, effective treatments for sickle cell anemia remain elusive.

Purpose of the Study:

  • To elucidate residue-level interactions stabilizing HbS polymers.
  • To explain the mechanism of polymerization inhibition in oxy HbS.
  • To investigate molecular insights into polymerization inhibition by glutathionyl HbS.

Main Methods:

  • Analysis of noncovalent interactions within HbS polymers.
  • Characterization of polymerization inhibition mechanisms.
  • Investigation of posttranslational modification (glutathionylation) effects on HbS.

Main Results:

  • Detailed description of intra- and inter-strand interactions stabilizing HbS polymers.
  • Demonstration of polymerization inhibition by the oxy form of HbS.
  • Identification of molecular insights into polymerization inhibition by glutathionyl HbS, even in the deoxy state.

Conclusions:

  • Elevating glutathionylation of HbS within RBCs, without oxidative stress, presents a potential therapeutic strategy for sickle cell anemia.
  • Understanding HbS polymerization inhibition mechanisms is crucial for developing new treatments.
  • Further research into posttranslational modifications of HbS could yield novel therapeutic targets.