[The proline biosynthesis gene proA from the thermophilic bacterium Thermus ruber: its cloning, sequencing and heterologous expression].

The proA proline biosynthesis gene of thermophilic bacterium Thermus ruber was cloned and sequenced, and several properties of the encoded enzyme, gamma-glutamylphosphate reductase (GPR) were studied. The proA open reading frame (ORF) was of 1286 bp. Nucleotide sequence analysis revealed the ATG initiation codon in position 36 and the TTA termination codon in position 1304.

[Denatured transitions of the molecular chaperone GroEL from Escherichia coli].

Conformational changes of oligomeric particle of GroEL chaperone from E. coli in solution were studied, which proceed during its denaturation upon the action of elevated urea concentration, temperature, and extremal pH values by the methods of CD, light scattering, scanning microcalorimetry, hydrophobic probe binding, and ATPase activity measurements. The ranges of changing the external conditions; within which GroEL retains its structure and functions, were determined.