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Valine (symbol Val or V) [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH 3 + form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain isopropyl group, making it a non-polar aliphatic amino acid.
The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and to be excluded by water. [1][2] The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes the entropy of water and minimizes the area of contact between ...
Fluid mosaic model of a cell membrane. The fluid mosaic model explains various characteristics regarding the structure of functional cell membranes.According to this biological model, there is a lipid bilayer (two molecules thick layer consisting primarily of amphipathic phospholipids) in which protein molecules are embedded.
The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates a "hydrophobic patch" on the protein surface that promotes intermolecular aggregation, the molecular event that gives rise to [sickle-cell anemia].
For example, the sickle-cell trait is caused by a single mutation of an adenine to a thymine in the hemoglobin gene, causing a switch from a glutamic acid to a valine. [16] This completely changes the three-dimensional structure of hemoglobin and thus changes the physical properties of the protein that lead to the sickle-cell trait.
Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. [1] The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the ...
In chemistry, a salt bridge is a combination of two non-covalent interactions: hydrogen bonding and ionic bonding (Figure 1). Ion pairing is one of the most important noncovalent forces in chemistry, in biological systems, in different materials and in many applications such as ion pair chromatography.
Interbilayer forces in membrane fusion. Membrane fusion is a key biophysical process that is essential for the functioning of life itself. It is defined as the event where two lipid bilayers approach each other and then merge to form a single continuous structure. [ 1] In living beings, cells are made of an outer coat made of lipid bilayers ...