Search results
Results from the WOW.Com Content Network
Further hemoglobin crystal structures at higher resolution (PDB 1MHB, 1DHB) soon showed the coupled change of both local and quaternary conformation between the oxy and deoxy states of hemoglobin, [5] which explains the cooperativity of oxygen binding in the blood and the allosteric effect of factors such as pH and DPG. For decades hemoglobin ...
A giant cell (also known as a multinucleated giant cell, or multinucleate giant cell) is a mass formed by the union of several distinct cells (usually histiocytes), often forming a granuloma. [ 1 ] Although there is typically a focus on the pathological aspects of multinucleate giant cells (MGCs), they also play many important physiological roles.
Example of platelets release in mature megakaryocytes. This footage shows the formation and spontaneous release of platelets (small round-shaped blood cells), imaged with a live-cell imaging microscope. Thrombopoietin (TPO) is a 353-amino acid protein encoded on chromosome 3p27.
Examples of inclusions are glycogen granules in the liver and muscle cells, lipid droplets in fat cells, pigment granules in certain cells of skin and hair, and crystals of various types. [3] Cytoplasmic inclusions are an example of a biomolecular condensate arising by liquid-solid, liquid-gel or liquid-liquid phase separation.
Found in many annelids, including earthworms, it is a giant free-floating blood protein containing many dozens—possibly hundreds—of iron- and heme-bearing protein subunits bound together into a single protein complex with a molecular mass greater than 3.5 million daltons. Leghemoglobin
For example, while biology refers to macromolecules as the four large molecules comprising living things, in chemistry, the term may refer to aggregates of two or more molecules held together by intermolecular forces rather than covalent bonds but which do not readily dissociate.
Inclusion bodies have a non-unit (single) lipid membrane [citation needed].Protein inclusion bodies are classically thought to contain misfolded protein.However, this has been contested, as green fluorescent protein will sometimes fluoresce in inclusion bodies, which indicates some resemblance of the native structure and researchers have recovered folded protein from inclusion bodies.
Developing protein crystals is a difficult process influenced by many factors, including pH, temperature, ionic strength in the crystallization solution, and even gravity. [3] Once formed, these crystals can be used in structural biology to study the molecular structure of the protein, particularly for various industrial or medical purposes. [4 ...