[Oligomerization of site-specific nicking endonuclease BspD6I at high protein concentrations].

Ability of site-specific nickase BspD6I (Nt.BspD6I) to oligomerize at concentrations > or = 0.5 microM (> or = 0.

[Effect of single-stranded DNA binding proteins on template/primer-independent DNA synthesis in the presence of nicking endonuclease Nt.BspD6I].

In the presence of the Nt.BspD6I nicking endonuclease DNA polymerase Bst stimulates intensive template/primer-independent DNA synthesis. Template/primer-independent DNA synthesis could be the reason for appearing nonspecific DNA products in many DNA amplification reactions particularly in the reactions with using nicking endonucleases.

[Effect of various humidity on local dynamic structure of lysozyme in a spin-labeled tetragonal crystal].

The dynamics of the side groups of amino acid residues and local conformational changes in the lysozyme molecule upon dehydration and rehydration of lysozyme crystals were studied by the methods of spin label, X-ray diffraction, and molecular dynamics. The His15 residue of lysozyme from chicken egg white was modified by spin label, and spin-labeled tetragonal crystals of the protein were grown. The spatial structure of the covalently bound spin label and its immediate surroundings in the lysozyme tetragonal crystal was determined.

[Dynamic mobility of the histidine-containing domain of spin-labeled lysozyme].

The hen egg-white lysozyme was modified by the spin label (2,2,6,6-tetramethylpiperidine-N1-oxyl-4-iodacetamide) at the single histidine residue His-15. The rotational correlation time of the molecular carrier was found to be defined by the mobility of the histidine-bearing domain and not influenced by the protein monomer shape at pH 4.7 and dimer shape at pH 7.