Natalia S Katina

  • Citations Per Year
Learn More
Influence of 12 nonpolar amino acids residues from the hydrophobic core of apomyoglobin on stability of its native state and folding intermediate was studied. Six of the selected residues are from the A, G and H helices; these are conserved in structure of the globin family, although nonfunctional, that is, not involved in heme binding. The rest are(More)
The interaction of apomyoglobin and its mutant forms with phospholipid membranes was studied using tryptophan fluorescence and circular dichroism in the far UV region. It is shown that a negatively charged phospholipid membrane can have a dual effect on the structure of protein molecule upon their interaction. On the one hand, the membrane induces(More)
Several research teams have reported detection and characterization of various apomyoglobin intermediate states different in their accumulation mode, thus putting a natural question as to proportions of these intermediates. The current report presents spectral properties of sperm whale apomyoglobin studied over a wide range of conditions with the use of(More)
Formation of amyloid-like protein aggregates in human organs and tissues underlies many serious diseases, therefore being in the focus of numerous biochemical, medical, and molecular biological studies. So far, formation of amyloids by globular proteins has been studied mostly under conditions that strongly destabilized their native structure. Here we(More)
Protein aggregation or misfolding in the cell is connected with many genetic diseases and can result from substitutions in proteins. Substitutions can influence the protein stability and folding rates in both intermediate and native states. The equilibrium urea-induced unfolding was studied for mutant apomyoglobins carrying substitutions of the conserved(More)
The contributions of some amino acid residues in the A, B, G, and H helices to the formation of the folding nucleus and folding intermediate of apomyoglobin were estimated. The effects of point substitutions of Ala for hydrophobic amino acid residues on the structural stability of the native (N) protein and its folding intermediate (I), as well as on the(More)
  • 1