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The hydrophobic effect is the desire for non-polar molecules to aggregate in aqueous solutions in order to separate from water. [22] This phenomenon leads to minimum exposed surface area of non-polar molecules to the polar water molecules (typically spherical droplets), and is commonly used in biochemistry to study protein folding and other ...
Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. [1] An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO. [2]
Thus the inside of the bilayer sheet is a non-polar region sandwiched between the two polar sheets. [ 2 ] Although phospholipids are the principal constituents of biological membranes, [ 3 ] there are other constituents, such as cholesterol and glycolipids , which are also included in these structures and give them different physical and ...
False-color Cassini radar mosaic of Titan's north polar region; the blue areas are lakes of liquid hydrocarbons. "The existence of lakes of liquid hydrocarbons on Titan opens up the possibility for solvents and energy sources that are alternatives to those in our biosphere and that might support novel life forms altogether different from those on Earth."—NASA Astrobiology Roadmap 2008 [1]
For example, the biotin-streptavidin interaction can be broken by incubating the complex in water at 70 °C, without damaging either molecule. [6] An example of change in local concentration causing dissociation can be found in the Bohr effect , which describes the dissociation of ligands from hemoglobin in the lung versus peripheral tissues.
Binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and Van der Waals forces. The association or docking is actually reversible through dissociation. Measurably irreversible covalent bonding between a ligand and target molecule is atypical in biological systems.
In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site.
On the molecular level, the interlocked molecules cannot be separated without the breaking of the covalent bonds that comprise the conjoined molecules; this is referred to as a mechanical bond. Examples of mechanically interlocked molecular architectures include catenanes , rotaxanes , molecular knots , and molecular Borromean rings .