Protein folding: Difference between revisions
imported>Mitchell McGill No edit summary |
imported>Mitchell McGill No edit summary |
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Viscosity-Collision. | Viscosity-Collision. | ||
Etc. | Etc. | ||
== Thermodynamics == | == Thermodynamics == |
Revision as of 13:14, 31 December 2008
Proteins are large molecules composed of smaller constituents called amino acids. They are ubiquitous and essential for all life. The 3-dimensional structure and the function of a protein are intimately related. The process by which a protein achieves a final structure is referred to as protein folding.
In cells, genes encoded in DNA are transcribed into messenger RNA (mRNA). The mRNA can then be translated into an amino acid chain called a polypeptide (after the peptide bond connecting the amino acids). From here, the polypeptide must find and adopt a 3-dimensional conformation.
History of Protein Folding as a Field
C. Anfinsen. K. Dill. Etc.
Proposed Mechanisms
Hydrophobic Collapse. Nucleation-condensation. Viscosity-Collision. Etc.
Thermodynamics
Folding Funnel/Energy Landscapes. Etc.
Chaperones
Chaperones make up a unique class of proteins which can aid in the proper folding of other proteins. For more information, see Chaperone Proteins.
Related Diseases and Disorders
Alzheimer's. Prion Disease(s). Transmissable Spongiform Encephalopathies (Creutzfeldt-Jakob Disease). Parkinson's Disease. Huntington's Disease. Amyotrophic Lateral Sclerosis.