Biocurious

/ a biophysics blog

Protein calms the waters

Posted 20 November 2007 by Andre under

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.

The rest of the article is here and the original article is available from the author’s website [pdf].

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.

  

  1. Doug    20 November 07    #

    Hi Andre,

    When I view the helices of ionic proteins or nucleic acids, I still wonder if there is some type of solenoid-like activity to assist in explaining these phenomena?

    Could these be a liquid [water] solenoid?

    See HyperPhysics – R Nave – GSU
    Bar Magnet and Solenoid
    and
    Iron Core Solenoid [contrasted with air solenoid]
    http://hyperphysics.phy-astr.gsu.edu/hbase/magnetic/elemag.html


  2. Joshua    21 November 07    #

    Here’s another interesting piece about the dynamics of water around a protein . . .
    http://scitation.aip.org/journals/doc/JCPSA6-ft/vol_127/iss_4/045101_1.html


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