Covalent attachment of myristate occurs on a wide variety of viral and cellular proteins. This modification is often essential for the proper functioning of the modified protein. The myristoylation plays an important role in protein-lipid interactions, which are modulated by the interplay between protein phosphorylation and calmodulin. Myristoylation is also involved in protein-protein interactions. In this review, recent advances in understanding the role of protein myristoylation in both protein-lipid and protein-protein interactions and the regulation of these interactions will be discussed on the basis of the structural studies.
Protein nanomachines have many attractive features. Whether we can take advantage of those depends on future technical advancements to reconstitute their functions in vitro in a useful manner. Breakthroughs towards this direction have been made in the field of protein molecular motors. In addition, novel challenges are recently initiated to use cells or organelles with superb motility as micro actuators or carriers, in conjunction of their genetic modifications.
From the viewpoint of the sequence space, the protein folding problem can be regarded as a problem of searching for the determinants of protein foldability. The concept of “folding elements (FEs)” has emerged from the search for the amino acid sequence essential for a protein to be foldable. Here we review the characteristics of the FEs of a small globular protein, dihydrofolate reductase, and the necessary conditions for the protein to be foldable. We also review the relationship between the FEs and the kinetic folding reaction and propose the FE-assembly model of protein folding.