Anfinsen dogma
The Anfinsen dogma (also the thermodynamic hypothesis of protein folding ) postulates that every protein under physiological conditions has a native protein fold with minimal free energy , which is predetermined by the amino acid sequence. The minimum energy can be displayed graphically using a folding funnel. The postulate was formulated by Nobel laureate Christian B. Anfinsen based on his studies on ribonuclease A.
properties
Anfinsen formulated three conditions:
- Uniqueness - Each amino acid sequence has only one minimal free energy conformation
- Stability - Insensitivity to minor changes in the environment due to the energetically most favorable folding
- Kinetic accessibility - There must not be excessive activation energies between the individual folding steps
Borderline cases of the Anfinsen dogma are e.g. B. prions and proteins that require chaperones for protein folding. The POEM @ home software uses parts of the Anfinsen dogma to predict protein structure .
The Levinthal Paradox describes the increasing complexity of protein folding to achieve a certain protein structure with increasing chain length.
Individual evidence
- ↑ CB Anfinsen: Principles that govern the folding of protein chains . In: Science . 181, No. 4096, 1973, pp. 223-230. doi : 10.1126 / science.181.4096.223 . PMID 4124164 .
- ↑ FH White: Regeneration of native secondary and tertiary structures by air oxidation of reduced ribonuclease . In: J. Biol. Chem. . 236, 1961, pp. 1353-1360. PMID 13784818 .
- ↑ CB Anfinsen, E. Haber, M. Sela, FH Jr. White: The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain . In: PNAS . 47, No. 9, 1961, pp. 1309-1314. doi : 10.1073 / pnas.47.9.1309 . PMID 13683522 . PMC 223141 (free full text).