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The tight interaction between the small molecule biotin and the tetrameric protein streptavidin is widely exploited for many different applications in protein science. In this issue, researchers present the design of a monovalent streptavidin tetramer with a single biotin binding site and demonstrate its enhanced properties over wild-type streptavidin for use in cell-surface protein labeling.
A new approach to generating large quantities of myeloid progenitor cells ex vivo will facilitate detailed studies of normal white blood cell differentiation and of abnormalities leading to blood disorders such as leukemia.
Proteins can be subjected to a wide variety of targeted post-translational modifications that will considerably modulate their function. Fortunately, several new technologies have emerged to assist in identification and analysis of these modifications, shedding new light on an important layer of proteomic complexity. Caitlin Smith reports.
