| Abstrakt: |
Major results of the use of protein engineering methods in studies of calcium-binding proteins with the highest affinity for calcium and known three-dimensional structure (parvalbumin, calmodulin, troponin C, calbindin, recoverin, alpha-lactalbumin, and others) are presented. Specific features of recombinant calcium-binding proteins are discussed. Experiments with genetic introduction of fluorescent probes, tryptophan and tyrosine, into proteins are overviewed. Effects of mutations in different parts of protein molecules (calcium-binding loops, hydrophobic core, and others) on their structure and properties and attempts of creation of artificial calcium-binding sites are discussed. |
