Crystal structure and molecular interactions of tropomyosin.

The three-dimensional structure of tropomyosin filaments has been determined by X-ray crystallography. The ends of the molecules were located by reference to the single pair of cysteine residues. Departures from the alpha-helical-coiled coil conformation may occur in localised domains along the molecule as well as at the overlapping ends.     

Replication of immune RNA by human lymphoblastoid cells]

Animal immune RNA used for the induction of the human lymphoblastoid cell line LDV/7, induces the appearance of receptor sites on the surface of these cells and the synthesis of specific immunoglobulins which are liberated into the culture medium. Furthermore, RNA has been extracted from these cells, which possesses the same properties of specific cytotoxicity as the RNA used for induction. It is supposed that the immune RNA derepresses specific genes on the genome of the induced cells.     

Alpha-lactalbumin possesses a novel calcium binding loop

Calcium performs a unique role in biology, achieving biological effects through highly specific interactions with and modulation of target proteins. It has been proposed that calcium-modulated proteins possess a characteristic, evolutionarily related, binding fold, known as the EF-hand. The high-resolution X-ray structure of alpha-lactalbumin reveals a Ca2+ binding fold that resembles an EF-hand only superficially and presumably has no evolutionary relationship with it. However, there is clear homology with the corresponding loop in c-type lysozyme (the 'parent' molecule of alpha-lactalbumin). This study, at 1.7 A resolution, represents one of the most accurate analyses of a calcium binding protein yet reported.