Crystal structure of a foldamer reported by Lehn and coworkers in Helv. Chim. Acta., 2003, 86, 1598-1624.

In chemistry folding is the process by which a molecule assumes its shape or conformation. The process can also be desribed as intramolecular self-assembly where the molecule is directed to form a specific shape through noncovalent interactions, such as hydrogen bonding, metal coordination, hydrophobic forces, van der Waals forces, pi-pi interactions, and/or electrostatic effects. Jean-Marie Lehn (born September 30, 1939) is a French chemist. ... Conformational isomerism is the phenomenon of molecules with the same structural formula but different conformations (conformers) of atoms about a rotating bond. ... An example of a molecular self-assembly through hydrogen bonds reported by Meijer and coworkers in Angew. ... An example of a quadruple hydrogen bond between a self-assembled dimer complex reported by Meijer and coworkers. ... The hydrophobic effect is the property that nonpolar molecules like to self-associate in the presence of aqueous solution. ... In chemistry, the term van der Waals force originally referred to all forms of intermolecular forces; however, in modern usage it tends to refer to intermolecular forces that deal with forces due to the polarization of molecules. ... In supramolecular chemistry, a π-π interaction is a non-covalent interaction as well hydrogen bonds, van der Waals forces, charge-transfer interactions, and dipole-dipole interactions. ...

The most active area of interest in the folding of molecules is the process of protein folding, which is the shape that is assumed by a specific sequence of amino acids in a protein. The shape of the folded protein can be used to understand its function and design drugs to influence the processes that it is involved in. Protein folding is the process by which a protein assumes its characteristic functional shape or tertiary structure, also known as the native state. ... In chemistry, an amino acid is any molecule that contains both amino and carboxylic acid functional groups. ...

There is also a great deal of interest in the construction of artificial folding molecules or foldamers. They are studied as models of biological molecules and potential application to the development of new functional materials. A foldamer is a discrete chain molecule or oligomer that adopts a secondary structure stabilized by non-covalent interactions . They are artificial molecules that mimic the ability of proteins, nucleic acids, and polysaccharides to form well-defined conformations, such as helices and ß-sheets. ...

See also

• Molecular self-assembly
• Foldamers
• Protein folding
• Secondary structure
• Tertiary structure

An example of a molecular self-assembly through hydrogen bonds reported by Meijer and coworkers in Angew. ... A foldamer is a discrete chain molecule or oligomer that adopts a secondary structure stabilized by non-covalent interactions . They are artificial molecules that mimic the ability of proteins, nucleic acids, and polysaccharides to form well-defined conformations, such as helices and ß-sheets. ... Protein folding is the process by which a protein assumes its characteristic functional shape or tertiary structure, also known as the native state. ... A representation of the 3D structure of the Myoglobin protein. ... In biochemistry, the tertiary structure of a protein is its overall shape. ...

References

1. A Field Guide to Foldamers. Hill, D. J.; Mio, M. J.; Prince, R. B.; Hughes, T.; Moore, J. S. Chem. Rev. 2001, 101, 3893-4011 DOI:10.1021/cr990120t. A digital object identifier (or DOI) is a standard for persistently identifying a piece of intellectual property on a digital network and associating it with related data, the metadata, in a structured extensible way. ...