He then became affiliated with the Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, first as Research Assistant, then as Research Associate, and later as Associate Professor. While he was a Research Associate, he did a postdoctoral fellowship in the Department of Microbiology of the Biozentrum at Basel University in Switzerland. Later Dr. Mesyanzhinov received his D.Sc. Prior to attaining his current position, he held an appointment at the Ivanovsky Institute of Virology of the Academy of Medical Sciences, Moscow. Dr. Mesyanzhinov is collaborating with Michael G. Rossman, Ph.D., a Professor at Purdue University.
Large loops connect the domains.
The region formed by loops between the amino-terminal domain and the middle domain provide the protein with conformational flexibility that may be essential to permit gp9 to perform as a trigger for the T4 tail contraction in the first stage of viral infection. Similarly, the partially coiled coil structure of the gp9 amino-terminal domain is more likely to be associated with the trimeric proximal part of the long tail fibers. A combination of the complementary techniques, protein engineering, molecular genetics, and X-ray crystallography is being used to study the folding of fibritin. These loops are rigid structures that do not interfere with the continuation of the alpha-helices at either side. The loops start and finish with glycine residues.