Electrostatic force driven conformational change in Fatty Acid Binding Protein
Fatty acid binding proteins (FABP) are a class of cytoplasmic proteins that bind to long-chain fatty acid. Their major role includes shuttling of free fatty acid to appropriate organelles for different metabolic fates within the cell. FABP is important to fatty acid trafficking due to the low solubility of fatty acid, a common characteristic of molecules with long hydrocarbon chain. To overcome this obstacle, fatty acids binds to FABP to enhance their aqueous solubility and facilitate intracellular lipid transportation.
Fatty acid has been found to enter the nucleus and regulate gene transcription through the interaction with nuclear receptor protein. Fatty acid serves as a signaling molecule of peroxisome proliferator-activated receptors (PPAR), which a group a nuclear receptor protein capable of mediating gene transcription. Past researches have shown that the transported FABP:FA complex in the cytosol translocates into the nucleus and interacts with PPAR. FABP:FA complex releases the bound FA from its B-barrel binding pocket upon binding with PPAR in the nucleus. The binding of FA with PPAR initiates gene expression leading to chronic inflammation inhibition as shown in many clinical studies using mammalian models.
Despite the functional discoveries about FABP:FA complex, little is known about the biophysical forces behind the dynamics of ligand binding and release in the FABP. The FABP structure can be compared to the ones from lipocalin, which is a closely related structural homolog of FABP. Structural and conformational changes were detected in lipocalin during association with ligand binding and release. Like the structure homolog lipo...
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James Danilli intended to further explain in the Davson and danilli model observations on the surface tensions in the lipid bilayers and even though there were some flaws ...
Our chicken sandwich has, by now, been broken down into digestible nutrients. The pancreatic juices have broken down the carbohydrates in the bread into monosaccharides (such as glucose and galactose) which leave the enterocyte by facilitated diffusion and enter the rich network of capillaries. They are transported in the blood stream and cross into the cytoplasm by Na+ cotransporters. Amino acids are moved to the circulation by facilitated diffusion. Lipids from the butter are broken down into fatty acids by lipases and are then absorbed across the cell membrane into the cytosol where they are reassembled into lipoprotein particles called chylomicrons. These are carried through lymphatic channels and into the circulation via the thoracic duct. The bloodstream carries simple sugars, glycerol, amino acids, and a number of salts and vitamins to the liver. The lymphatic system, a network of vessels that carry white blood cells and lymph fluid throughout the body, absorbs fatty acids and
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Fatty acids are another type of lipid. The common feature of fatty acids is that they are all esters of moderate to long chain fatty acids. Two polyunsaturated fatty acids, linoleic and linoleic, are designated "essential" because their absence in the human diet has been associated with health problems, such as scaly skin, stunted growth and increased dehydration. These acids are also precursors to the prostaglandins, a family of physiologically potent lipids present in minute amounts in most body tissues.
Proteins are considered to be the most versatile macromolecules in a living system. This is because they serve crucial functions in all biological processes. Proteins are linear polymers, and they are made up of monomer units that are called amino acids. The sequence of the amino acids linked together is referred to as the primary structure. A protein will spontaneously fold up into a 3D shape caused by the hydrogen bonding of amino acids near each other. This 3D structure is determined by the sequence of the amino acids. The 3D structure is referred to as the secondary structure. There is also a tertiary structure, which is formed by the long-range interactions of the amino acids. Protein function is directly dependent on this 3D structure.
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There are four main levels of a protein, which make up its native conformation. The first level, primary structure, is just the basic order of all the amino acids. The amino acids are held together by strong peptide bonds. The next level of protein organization is the secondary structure. This is where the primary structure is repeated folded so that it takes up less space. There are two types of folding, the first of which is beta-pleated sheets, where the primary structure would resemble continuous spikes forming a horizontal strip. The seco...
In the hierarchial organisation of proteins, domains are found at the highest level of tertiary structure. Since the term was first used by Wetlaufer (1973) a number of definitions exist reflecting author bias, however all of the definitions agree that domains are independently folding compact units. Domains are frequently coded by exons and therefore have specific functionality. Among the many descriptions of protein domains the two most striking and simple are " Protein evolutionary units" and "Basic currency of Proteins".
a. TERMINAL LEARNING OBJECTIVE: To familiarize you with the main components and characteristics of the 81mm mortar.
Useful for the military, projectile motion can now be used for a number of weapons; which is when an object (like a bullet or cannon) is thrown-projected- and mov...
...-membrane outer membrane proteins have lagged behind the studies of lipoproteins due to their aberrant behavior by Triton X-114 detergent fractionation. Due to this reason, trans-membrane outer membrane proteins can be best characterized by assessing membrane integration as well as surface exposure. Not surprisingly, some of the outer membrane proteins that are involved in mediating host–pathogen interactions are strongly regulated by the conditions that are found in mammalian host tissues. For instance, the leptospiral immunoglobulin-like repeat proteins are dramatically induced by the osmolarity and they would mediate the interactions with host extracellular matrix proteins. Development of latest molecular tools in genetics is making it possible to understand the roles of these and several other outer membrane proteins in the mechanism of leptospiral pathogenesis.