Fluorescence approach to evaluating conformational changes upon binding of beta-spectrin ankyrin-binding domain mutants with the lipid bilayer.

The major component of the cell membrane skeleton, spectrin, is anchored in the cell membrane via interactions with membrane proteins. It has been previously shown that both erythroid and non-erythroid spectrin interact directly with membrane phospholipids (mainly aminophospholipids). One of the binding sites responsible for these interactions is located in the ankyrin-binding domain.

A method to evaluate the effect of liposome lipid composition on its interaction with the erythrocyte plasma membrane.

Lipid aggregates are considered promising carriers for macromolecules and toxic drugs. In order to fulfill this function, aggregates should have properties that ensure the efficient delivery of their cargo to the desired location. One of these properties is their stability in blood when accumulating in the targeted tissue.

Analysis of scanning force microscopy images of protein-induced DNA bending using simulations.

Bending of DNA is a feature essential to the function of many DNA-binding proteins. Bending angles can be estimated with a variety of techniques, but most directly from images obtained using scanning force microscopy (SFM). Direct measurement of the bending angle using a tangent method often produces angles that deviate significantly from values obtained using other techniques.

The kinetics of haemolysis of spherocytic erythrocytes.

Spherocytosis is a hereditary disease. It results from mutations in genes that encode proteins participating in the attachment of the membrane skeleton to the plasma membrane bilayer of the erythrocyte. In affected cells, interaction between the spectrin-actin meshwork and integral membrane proteins is altered.