Folding (chemistry)
Encyclopedia
In chemistry, folding is the process by which a molecule assumes its shape or conformation
. The process can also be described 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 force
s, pi-pi interactions, and/or electrostatic effects.
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.
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.
Conformational isomerism
In chemistry, conformational isomerism is a form of stereoisomerism in which the isomers can be interconverted exclusively by rotations about formally single bonds...
. The process can also be described as intramolecular self-assembly
Molecular self-assembly
Molecular self-assembly is the process by which molecules adopt a defined arrangement without guidance or management from an outside source. There are two types of self-assembly, intramolecular self-assembly and intermolecular self-assembly...
where the molecule is directed to form a specific shape through noncovalent interactions, such as hydrogen bonding
Hydrogen bond
A hydrogen bond is the attractive interaction of a hydrogen atom with an electronegative atom, such as nitrogen, oxygen or fluorine, that comes from another molecule or chemical group. The hydrogen must be covalently bonded to another electronegative atom to create the bond...
, metal coordination, hydrophobic forces
Hydrophobic effect
The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in aqueous solution and exclude water molecules. The name, literally meaning "water-fearing," describes the segregation and apparent repulsion between water and nonpolar substances...
, van der Waals force
Van der Waals force
In physical chemistry, the van der Waals force , named after Dutch scientist Johannes Diderik van der Waals, is the sum of the attractive or repulsive forces between molecules other than those due to covalent bonds or to the electrostatic interaction of ions with one another or with neutral...
s, pi-pi interactions, and/or electrostatic effects.
The most active area of interest in the folding of molecules is the process of protein folding
Protein folding
Protein folding is the process by which a protein structure assumes its functional shape or conformation. It is the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure from random coil....
, 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.
There is also a great deal of interest in the construction of artificial folding molecules or foldamers
Foldamers
A foldamer, is a discrete chain molecule or oligomer that adopts a secondary structure stabilized by noncovalent interactions. They are artificial molecules that mimic the ability of proteins, nucleic acids, and polysaccharides to fold into well-defined conformations, such as helices and β-sheets...
. They are studied as models of biological molecules and potential application to the development of new functional materials.
See also
- Molecular self-assemblyMolecular self-assemblyMolecular self-assembly is the process by which molecules adopt a defined arrangement without guidance or management from an outside source. There are two types of self-assembly, intramolecular self-assembly and intermolecular self-assembly...
- FoldamersFoldamersA foldamer, is a discrete chain molecule or oligomer that adopts a secondary structure stabilized by noncovalent interactions. They are artificial molecules that mimic the ability of proteins, nucleic acids, and polysaccharides to fold into well-defined conformations, such as helices and β-sheets...
- Protein foldingProtein foldingProtein folding is the process by which a protein structure assumes its functional shape or conformation. It is the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure from random coil....
- Secondary structureSecondary structureIn biochemistry and structural biology, secondary structure is the general three-dimensional form of local segments of biopolymers such as proteins and nucleic acids...
- Tertiary structureTertiary structureIn biochemistry and molecular biology, the tertiary structure of a protein or any other macromolecule is its three-dimensional structure, as defined by the atomic coordinates.-Relationship to primary structure:...