zbu at ccny dot cuny dot edu
Looking for a
WELL-COMPENSATED
job?
My main page is
HERE!
Nanoscale
protein dynamics:
A new
frontier
for neutron spin echo spectroscopy
Neutron spin echo
spectroscopy
(NSE)
is the
only experimental technique
that can determine protein motion on nano length and time scales.
Such motions have long been hypothesized to be the most significant modes for protein function.
We have developed a theoretical framework that allows one to interpret the NSE data.
Our theoretical framework uses simple concepts from
nonequilibrium statistical mechanics,
and does not require elaborate molecular dynamics simulations, complex fits to rotational motion,
or elastic network models. In combination with our experimental methodology of selective deuterium
labeling, our work clears significant hurdles to the understanding of this very important problem.
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Assembling amyloid fibrils from designed structures
containing a significant Alzheimer beta-peptide fragment.
L.O. Tjernberg,
A. Tjernberg,
N. Bark,
Y. Shi,
B. P. Ruzsicska,
Z. Bu,
J. Thyberg,
D.J.E. Callaway.
Biochem. J. (2002) 366, 343-351.
Shi Y, Stouten PF,
Pillalamarri N, Barile L,
Rosal RV, Teichberg S, Bu Z,
D.J.E. Callaway.
Quantitative determination
of the topological propensities
of amyloidogenic peptides.
Biophys Chem. 120 (2006), 55-61.
Bu Z, Shi Y,
D.J.E. Callaway, {co-corresponding},
and Tycko R.
Molecular alignments within
beta-sheets in Abeta(14-23) fibrils:
solid-state NMR experiments and theoretical predictions.
Biophys J. 2007 92: p. 594-602.