Opposites Attract in a Motor Protein
experimentalists, computational biologists investigated how two myosin VI assemble and pull their cargo together. The investigation, reported recently, focused on a segment of myosin VI that forms a long,rigid alpha-helix that is notably decorated with a distinct rings of positively and negatively charged amino acids. Carrying out single-molecule experiments along with molecular dynamics simulations using NAMD, it was found out that two myosin VI proteins attract each other electrostatically through the charge-ring proteins, shifting them such that the oppositely charged amino acids from different helices face each other. More information can be found on our motor protein website.