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Nanosecond Dynamics of Calmodulin and Ribosome-bound Nascent Chains Studied by Time-Resolved Fluorescense Anisotropy

In protein biosynthesis the coupling between polypeptide chain elongation and protein folding is one of the key issues of this vital cellular process. We employ an experimental approach to analyze structural and dynamical properties of nascent polypeptide chains which were synthesized using cell-free expression systems to different length. In this approach we studied calmodulin by measuring time-resolved anisotropy decays and identified a pronounced interaction of the nascent chains with the synthesizing ribosome. (Lamprou et al., ChemBioChem 2014, 15, 977-985)


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