my husband, the scientist

It's a pretty big deal to get a paper published in the scientific community. Wade has only had a few published during his 5 years as a graduate student (which is pretty normal) and the following is an abstract from his final paper during that time, which was just published in the Journal of Bimolecular NMR. So, congratulations Wade for your hard work!

Use of reverse micelles in membrane protein structural biology
Wade D. Van Horn Æ Mark E. Ogilvie Æ Peter F. Flynn

Membrane protein structural biology is a rapidly
developing field with fundamental importance for elucidating
key biological and biophysical processes including
signal transduction, intercellular communication, and cellular
transport. In addition to the intrinsic interest in this area
of research, structural studies of membrane proteins have
direct significance on the development of therapeutics that
impact human health in diverse and important ways. In this
article we demonstrate the potential of investigating the
structure of membrane proteins using the reverse micelle
forming surfactant dioctyl sulfosuccinate (AOT) in application
to the prototypical model ion channel gramicidin A.
Reverse micelles are surfactant based nanoparticles which
have been employed to investigate fundamental physical
properties of biomolecules. The results of this solutionNMR
based study indicate that the AOT reverse micelle system is
capable of refolding and stabilizing relatively high concentrations
of the native conformation of gramicidin A.
Importantly, pulsed-field-gradient NMR diffusion and
NOESY experiments reveal stable gramicidin A homodimer
interactions that bridge reverse micelle particles. The
spectroscopic benefit of reverse micelle-membrane protein
solubilization is also explored, and significant enhancement
over commonly used micelle based mimetic systems is
demonstrated. These results establish the effectiveness of
reverse micelle based studies of membrane proteins, and
illustrate that membrane proteins solubilized by reverse
micelles are compatible with high resolution solution NMR
techniques.

(J Biomol NMR (2008) 40:203–211)