לוח שנה משולב

Explaining life in terms of the jiggling and wiggling of atoms is a central goal in modern biophysics. The dynamics of folded proteins include concerted motions of thousands of atoms, thus clearly exceeding the capabilities of analytical theories. On the other hand, intrinsically disordered proteins (IDPs) are well described by analytic polymer models of different flavors. Yet, these models are not applicable if disorder and order mix, e.g., for IDPs that form partially ordered complexes or for highly compact IDPs. Using single-molecule spectroscopy, we studied the dynamics of such ‘mixed’ cases and found that even weak interactions can tremendously slow down the IDP-dynamics. In the second part of the talk, I will demonstrate that such protein disorder is key for transmitting allosteric signals across many nanometers in DNA. An intrinsically disordered tail of a DNA-binding protein amplifies microsecond fluctuations in DNA and increases the chance of binding proteins at a distant site. These findings have implications for our understanding of transcription activation in gene expression and suggest a new functional role for IDPs in transcription factors. FOR THE LATEST UPDATES AND CONTENT ON SOFT MATTER AND BIOLOGICAL PHYSICS AT THE WEIZMANN, VISIT OUR WEBSITE: https://www.biosoftweizmann.com/