No new protein folding experiments were performed in FY2011. However, much effort was devoted to the development of new solid state NMR technology that will enable experiments in FY2012, particularly a new low-temperature magic-angle spinning probe with microwave irradiation capabilities that will enhance the sensitivity of protein folding measurements by a factor of at least 50 relative to our previously published results. In addition, we have initiated a collaboration with Prof. Victor Munoz to measure and interpret solution NMR chemical shifts and relaxation parameters in thermally unfolded HP35, using isotopically labeled protein samples that were synthesized in our laboratory in FY2011 and previous years.
|Hu, Kan-Nian; Tycko, Robert (2010) What can solid state NMR contribute to our understanding of protein folding? Biophys Chem 151:10-21|
|Hu, Kan-Nian; Yau, Wai-Ming; Tycko, Robert (2010) Detection of a transient intermediate in a rapid protein folding process by solid-state nuclear magnetic resonance. J Am Chem Soc 132:24-5|
|Hu, Kan-Nian; Havlin, Robert H; Yau, Wai-Ming et al. (2009) Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance. J Mol Biol 392:1055-73|