Entropy is one of the most interesting concepts in physics. If we define a state as a group of protein configurations separated by low energy barriers (~ 1 kT), we can relate entropy to the number of configurations of this state. The higher the number of configurations, the higher the entropy of this state.
Jose Caro, during his presentation at the Protein Dynamics and Allostery platform session on Sunday, presented a very interesting proposal to quantify entropy changes from experimental results. According to his presentation, most contributions to the entropy of a state come from protein motions in the picosecond timescale. This motions, in turn, can be detected by nuclear magnetic resonance (NMR) relaxation. A high order parameter (close to 1) indicates a rigid protein, while a low order parameter (close to 0) indicates a flexible protein. His idea was to quantify entropy changes by scaling changes in the order parameter.
The poster section on Sunday was also very interesting. I had very nice discussions, and among them I highlight my conversation with Carsten Kutzner about the computational electrophysiology method. He is pretty passionate about his work at the Max Planck Institute for Biophysical Chemistry.
The poster section of today (Monday) was awesome! I met some former lab mates and friends from my six-month visit to the University of Pittsburgh last year, met a friend from a Gordon Conference, and also met totally by chance professor Alex Dickson, which has been doing a really nice work on pathway sampling.
The bad thing is: my networking cards from Quartzy are over. Quartzy, would you make me 20 cards next time?