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The three-dimensional structure of the bacteriophage T4 baseplate-tail tube complex based on cryo-EM reconstruction. The background image consists of electron microscope photographs of bacteriophage T4 stained with uranyl acetate or embedded in vitreous ice. See pages 688–693.
A recent study demonstrates that, when searching for the smallest active ribozymes, researchers may have thrown away parts that are important for functions.
Recent ensemble and single molecule manipulation studies highlight the mechanical nature of protein unfolding in vivo and, thus, the greater need to understand the response of proteins to mechanical force.
Don't prejudge the function of a domain based on its sequence. Two recent studies drive home this message and add the sterile-α motif (SAM) to the growing list of domains that are able to interact with both proteins and nucleic acids.
How does the C-terminal domain (CTD) of RNA polymerase II interact specifically with multiple targets? A recent paper describing the structure of this domain with a mRNA capping enzyme guanylyltransferase suggests that the CTD is a contortionist that, upon post-translational modification, adopts different configurations specifically recognized by its partners.
