Postdoctoral Research (2014 - ) 

Will be updated soon ... 

Graduate Research (2008 - 2014) 



The primary aim of my thesis work in the Wand Lab was to investigate the role played by protein conformational entropy in very high-affinity interactions (Kd < 1 nM). However, prior to addressing this question several issues concerning:


  1. Insight into the NMR-mediated measurement of conformational entropy
  2. Role played by the abundance of aromatic amino acids at the interfaces of high-affinity interactions

needed to be addressed. These were addressed in the following publications:


  1. Origins of NMR-measurement protein conformational entropy (Refer to this article)
  2. Banding of protein methyl side chain dynamics and implications for redistribution of conformational entropy (Refer to this article)
  3. 13C Isotopic labeling scheme to enable NMR-measurement of aromatic dynamics (Refer to this article)
  4. Liquid-like interior of protein revealed by aromatic side chain motions (Refer to this article)