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.     

Die Technik der Nukleinsäurehybridisierung und ihre Bedeutung für diagnostische Fragestellungen

Nucleic acid hybridization techniques (e.g., Southern blotting and in situ hybridization) gain increasing importance in laboratory medicine, as demonstrated by examples in this paper. The molecular basis of this approach to detect nucleic acids homologous to known DNA probes is explained. It is concluded that this technique has advantages in the detection of pathogens compared to other methods used in laboratory medicine.     

Chemische Reaktionen von Phenylarsinverbindungen

In an equilibrium reaction, phenylarsine dichloride (PFIFFIKUS) reacts rapidly with alcohols at room temperature to yield phenylarsine bisether and phenylarsine chloride ether. The reactions, however, are not quantitative. The derivatives were identified using mass spectrometry.