Globin
A family of proteins involved in oxygen transport and storage
Globin is a family of proteins that play a crucial role in the transport and storage of oxygen in various organisms. These proteins are characterized by their ability to bind oxygen molecules, a function that is essential for the survival of aerobic life forms. Globins are found in a wide range of species, from bacteria to humans, and are integral components of hemoglobin and myoglobin.
Structure
Globins are typically composed of a series of alpha helices that form a globular structure. This structure is stabilized by hydrophobic interactions and hydrogen bonds. The core of the globin protein contains a heme group, which is responsible for binding oxygen. The heme group consists of an iron ion held within a porphyrin ring, allowing it to reversibly bind oxygen molecules.
Function
The primary function of globins is to facilitate the transport and storage of oxygen. In vertebrates, hemoglobin is the most well-known globin, responsible for transporting oxygen from the lungs to tissues throughout the body. Myoglobin, another type of globin, is found in muscle tissues and serves to store oxygen, providing a reserve during periods of intense muscular activity.
Oxygen Binding
The ability of globins to bind oxygen is due to the presence of the heme group. When oxygen binds to the iron ion in the heme, it causes a conformational change in the protein, enhancing its affinity for additional oxygen molecules. This cooperative binding is a key feature of hemoglobin, allowing it to efficiently load and unload oxygen as needed.
Types of Globins
Globins are classified into several types based on their structure and function:
- Hemoglobin: Found in red blood cells, responsible for oxygen transport.
- Myoglobin: Found in muscle cells, responsible for oxygen storage.
- Neuroglobin: Found in the brain and nervous system, thought to protect neurons from hypoxia.
- Cytoglobin: Found in various tissues, its exact function is still under investigation.
Evolution
Globins have a long evolutionary history, with evidence suggesting that they originated from a common ancestral gene. Over time, gene duplication and divergence have led to the variety of globins observed today. This evolutionary process has allowed globins to adapt to the specific oxygen transport and storage needs of different organisms.
Clinical Significance
Mutations in globin genes can lead to a variety of hemoglobinopathies, such as sickle cell disease and thalassemia. These conditions result from abnormal globin protein structure or function, leading to impaired oxygen transport and various clinical symptoms.
Related pages
Globin
Transform your life with W8MD's budget GLP-1 injections from $125.
W8MD offers a medical weight loss program to lose weight in Philadelphia. Our physician-supervised medical weight loss provides:
- Most insurances accepted or discounted self-pay rates. We will obtain insurance prior authorizations if needed.
- Generic GLP1 weight loss injections from $125 for the starting dose.
- Also offer prescription weight loss medications including Phentermine, Qsymia, Diethylpropion, Contrave etc.
NYC weight loss doctor appointments
Start your NYC weight loss journey today at our NYC medical weight loss and Philadelphia medical weight loss clinics.
- Call 718-946-5500 to lose weight in NYC or for medical weight loss in Philadelphia 215-676-2334.
- Tags:NYC medical weight loss, Philadelphia lose weight Zepbound NYC, Budget GLP1 weight loss injections, Wegovy Philadelphia, Wegovy NYC, Philadelphia medical weight loss, Brookly weight loss and Wegovy NYC
|
WikiMD's Wellness Encyclopedia |
| Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates, categories Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD