University of Akron issued the following announcement.
Disordered proteins display an intriguing mix of entropic freedom and weak intra-chain interactions that underlie their biological roles. Motivated to understand that interplay, we carried out single-molecule force spectroscopy measurements on a model disordered protein construct, consisting of multiple repeats of the tail domain of a neurofilament protein. Unexpectedly, we found that the construct displays glassy behavior: a one-step change in the applied force leads to an extremely slow, logarithmic response in the chain extension. Further, the disordered chain exhibits a distinct memory effect (the Kovacs effect), in which the chain ‘remembers’ changes in force that occurred tens of seconds prior. To interpret this behavior, we turned to recent studies that showed similar dynamics in a completely different system—the glassy behavior of crumpled paper balls. I will discuss how the insight from crumpled paper gave us clues into the molecular processes at work in the protein system, ultimately revealing that the mechanisms of glassy kinetics in the disordered chain differ from those typically invoked to explain glassy behavior in structured proteins.
For further information, please contact Dr. Junpeng Wang at jwang6@uakron.edu.
Original source here.
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