Related Experiment Video
Updated: Jul 12, 2026
11:17
Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
Where is the weak linkage in the globin chain?
1Department of Laboratory Medicine, Faculty of Medicine, Chulalongkorn University, Bangkok, Thailand. wviroj@yahoo.com
International Journal of Nanomedicine
|August 28, 2007
Summary
This study used bioinformatics to find vulnerable positions in alpha and beta globin chains, aiding in predicting new hemoglobinopathies. Identifying these weak linkages helps understand inherited blood disorders.
Area of Science:
- Genomics
- Proteomics
- Bioinformatics
Background:
- Hemoglobinopathies are prevalent inherited blood disorders, particularly in tropical regions.
- Predicting protein structure and function, and identifying mutation hotspots, are key challenges in proteomics and structural genomics.
Purpose of the Study:
- To identify vulnerable positions in alpha and beta globin chains prone to mutations.
- To utilize bioinformatics for predicting potential new hemoglobinopathies.
Main Methods:
- Bioinformatics analysis of alpha and beta globin chains.
- Application of the GlobPlot tool to identify weak linkages in globin chains.
Main Results:
- Identified 22 vulnerable positions in the alpha globin chain (e.g., positions 3-8, 38-42).
- Identified 46 vulnerable positions in the beta globin chain (positions 61-146).
Conclusions:
- Weak linkages in globin chains can be effectively identified using bioinformatics.
- This approach provides valuable insights for predicting novel mutations leading to hemoglobinopathies.
Related Concept Videos
02:21Globular and Fibrous Proteins
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
02:21Globular and Fibrous Proteins
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
01:27Globular Proteins
In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
00:49Ligand Binding and Linkage
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
00:49Ligand Binding and Linkage
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
01:24Hemoglobin
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...
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...