Stability and self-organization of proteins.
X-ray crystallography and NMR provide insight into the three-dimensional structure of proteins at high resolution yielding a relatively small number of stable "topologies". Their free energies of stabilization are minute compared to the total molecular energy. Molecular adaptation to extremes of physical conditions at the protein level refers to marginal alterations of the intramolecular interactions; clearcut predictions with respect to the correlation of protein structure and protein stability are at present not possible. The acquisition of the native structure of proteins is determined by the kinetically accessible minimum of potential energy. The overall mechanism may be described as a hierarchical condensation with elements of secondary/super-secondary structure and subdomains/domains as intermediate stages. In the case of oligomeric and multimeric proteins, folding and association of subunits follow a consecutive uni-bimolecular mechanism, the kinetics of which can be simulated with high precision. The "code of protein folding" is still unknown.
Jaenicke
R
R
Institut für Biophysik und Physikalische Biochemie, Universität, Regensburg.
D004355:Drug Stability; D046911:Macromolecular Substances; D011487:Protein Conformation; D011506:Proteins
D046911:Macromolecular Substances; D011506:Proteins