To maintain optimal protein homeostasis within the cell, a complex interplay exists between factors determining the production, transport, and folding of nascent chains. Here we review the evidence for the structural and dynamical properties of nascent polypeptide chains as they emerge from the ribosome and that enable them to acquire their biologically active, three‐dimensional structures. In particular, we focus on the application of NMR spectroscopy, which is now emerging as a powerful technique to probe the behavior and properties of emerging nascent chains.
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Cabrita et al. (2010) studied this question.
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