Abstract
Single crystal X-ray diffraction and circular dichroism studies of protamine binding to a tRNA suggest that the protamine molecule changes its conformation from a random coil to a structure containing α helices on binding to tRNA, and that α-helical segment(s) of protamine bind approximately along a shallow groove of a double-helical portion of tRNA. Based on these observations, a structural model for nucleoprotamine is proposed.
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Warrant, R., Kim, SH. α-Helix–double helix interaction shown in the structure of a protamine-transfer RNA complex and a nucleoprotamine model. Nature 271, 130–135 (1978). https://doi.org/10.1038/271130a0
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DOI: https://doi.org/10.1038/271130a0
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