by Andre on 21 November 2007
Here’s my latest Physicsworld.com news story:
Living organisms contain both proteins and water and the complex interactions between the two are thought to be the driving force behind many biological processes.
Now, biophysicists in the US have discovered that a protein called myoglobin can coordinate the motion of surrounding water molecules, slowing them down significantly – perhaps to allow certain interactions to occur (PNAS 104 18461). The team has also shown that the motion of these water molecules can be associated with the shape and function of the protein – information that could improve computer simulations of protein dynamics and lead to a better understanding of diseases like Alzheimer’s and Parkinson’s, which involve drastic protein shape changes.
They measured the ultrafast decay of fluorescence from tryptophans after they were excited by femtosecond pulses of UV. To get information over the surface of the protein they did a tryptophan scan and I’m sure it was a lot of work to prepare all those mutants so it’s nice that they could see some systematic trends in hydration dynamics with local surface charge.
Since Philip is the one doing ultrafast protein stuff now we can ask him to comment.