Melissa Sharp: Probing the structure and dynamics of proteins using neutron scattering
Plats: Kemicentrum, Lecture hall F
A physical chemistry seminar by Dr. Melissa Sharp, Instrument Scientist at European Spallation Source ERIC, Lund.
To fully understand the function of proteins it is necessary to consider both their structure and dynamics. Neutron spin-echo spectroscopy (NSE) has been shown to be ideally suited to probe the slow dynamics of materials, since it gives access to the dynamics on the nanosecond-timescale, making it a very powerful tool when combined with other techniques.
In this talk I will show how we have used NSE and backscattering spectroscopy to probe the dynamics of biologically relevant systems, such as human serum albumin, a protein abundant in blood, which plays a key role in the transport of compounds such as nutrients, hormones and drugs. We are able to detect small changes in the internal dynamics of the protein upon binding of small molecules such as heme and myristic acid under physiologically realistic conditions.
Another example is the use of NSE combined with computer simulations to study of the internal dynamics of the mercuric ion reductase MerA, an enzyme responsible for catalysing the NADPH-dependent reduction of Hg(II) to the uncharged, and much less harmful, Hg(0).