Which structures do complex proteins adopt in solution? Konstanz biophysicists answer this question using the example of ubiquitin dimers as well as a new combination of high-resolution NMR spectroscopy and sophisticated computer simulations.
, which are linked to form long amino acid chains as specified by our genetic material. In our cells, these chains are not simply rolled up like strings of pearls, but fold into complex, three-dimensional structures. How a protein is folded decisively influences its function: It determines, for example, which other molecules a protein can interact with in the cell.
The reason: complex proteins often fold into several compact subunits, called domains, which in turn may be connected by flexible linkers. The more flexibly connected subunits are present, the more different "Through NMR spectroscopy, for example, we get information about the dynamic properties of such proteins. Complex, on the other hand, provide a good overview of the range of possible folds," explains Kovermann."So far, no general approach that comprehensively maps the dynamic and structural properties of multi-domain proteins had existed."
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