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Encyclopedia > Coiled coil

A coiled coil is a structural motif found in many proteins. It consists of 2-5 alpha-helices that are coiled together like the strands of a rope. Dimers and trimers are the most common ones. Coiled coils usually contain a repeated seven residue pattern called heptad repeats. In an unbranched, chain-like biological molecule, such as a protein or a strand of RNA, a structural motif is a three-dimensional structural element or fold within the chain, which appears also in a variety of other molecules. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... A diagram of the alpha helix structure of amino acids In proteins, the α helix is a major structural motif in secondary structure. ... Sucrose, or common table sugar, is composed of glucose and fructose. ...


Coiled coils are held together by hydrophobic forces. When two or more alpha-helices have repeating patterns of hydrophobic amino acid side chains, the most favorable way for them to conform in the water-filled environment of the cytoplasm is to wrap the hydrophobic strands against each other sandwiched between the hydrophylic amino acids. In chemistry, hydrophobic or lipophilic species, or hydrophobes, tend to be electrically neutral and nonpolar, and thus prefer other neutral and nonpolar solvents or molecular environments. ... In chemistry, an amino acid is any molecule that contains both amino and carboxylic acid functional groups. ... Cytoplasm is the colloidal, semi-fluid matter contained within the cells plasma membrane, in which organelles are suspended. ...


  Results from FactBites:
 
Genome Biology | Full text | Predicting specificity in bZIP coiled-coil protein interactions (5898 words)
Coiled coils are found in proteins that participate in many diverse processes, including transcription, oncogenesis and membrane fusion; predicting protein-protein interactions mediated by this motif will have important biological ramifications.
Coiled-coil sequences are taken from a database of non-redundant interacting coiled coils containing approximately 29,000 residues from one of two classes: homodimeric coiled coils in myosin, tropomyosin, cortexillin and types III and V intermediate filament proteins; and heterodimeric coiled coils in keratin proteins [8,24].
Each of these studies [14,16,19,38,39,44-47] provides an ordering of the stabilities of the coiled coils considered, and thus constraints of the type in equation 2 are introduced.
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