|PhD||Harvard University||Cambridge, Mass.||Physics|
CAREER Award, National Science Foundation, 2011
Single molecule biophysics:
We enjoy addressing fundamental problems in biophysics via precision single-molecule measurement apparatus. Specifically, we are developing and implementing a unique ultrastable atomic force microscope (AFM) to elucidate the structure, structural energetics, and conformational fluctuations of membrane proteins. A central question is: How does the dynamic structure of these proteins influence their function? An ultrastable AFM complements traditional characterization techniques by providing an atomically precise means to address this question in physiologically relevant conditions.
Churnside AB, Sullan RM, Nguyen DM, Case SO, Bull MS, King GM, Perkins TT. Routine and timely sub-picoNewton force stability and precision for biological applications of atomic force microscopy. Nano Lett. 2012 Jul 11;12(7):3557-61. doi: 10.1021/nl301166w. Epub 2012 Jun 15.
Churnside AB, King GM, Perkins TT. Label-free optical imaging of membrane patches for atomic force microscopy. Opt Express. 2010 Nov 8;18(23):23924-32. doi: 10.1364/OE.18.023924.
G.M. King, A.R. Carter, A.B. Churnside, L.S. Eberle, and T.T. Perkins, Ultrastable atomic force microscopy: atomic-scale stability and registration in ambient conditions; Nano Letters 9, 1451 (2009).
A.R. Carter, G.M. King, and T.T. Perkins, Back-scattered detection provides atomic-scale localization precision, stability, and registration in 3D; Optics Express 15, 13434 (2007).
A.R Carter, G.M. King, T.A. Sheard, W. Halsey, D. Alchenberger & T.T. Perkins, Stabilization of an optical microscope to 0.1 nm in 3D; Applied Optics 46, 421 (2007).