Research
Nien-Hui Ge Group
Chemistry, UC Irvine
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Research
Nien-Hui Ge Group Chemistry, UC Irvine |
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Detailed knowledge of molecular
structures and dynamics in condense phases is essential to a complete and
predictive understanding of chemical and biological processes. Our research
program is directed to determine how molecular structures change in time, at
equilibrium and during reactions. Topics of current interest include: the
backbone and side chain conformation of peptides and proteins, kinetics of
protein folding, and local structure and dynamics of liquids. These endeavors
lead us to devise new techniques in nonlinear spectroscopy that can provide
detailed information on the time dependence of intra- and intermolecular
vibrational couplings, and hence structural changes as they evolve.
Ultrafast multidimensional multicolor IR spectroscopy. We are exploiting
new experimental techniques that are vibrational analogues of multidimensional
NMR. The extension beyond a single dimension gives these techniques the ability
to disentangle structural information from complex spectra where the couplings,
correlations, and relative angular orientations between structural units are
revealed as "cross peaks". Moreover, the picosecond time resolution of
multidimensional IR makes it an ideal structural probe for short-lived
intermediates in chemical or biological processes once initiated by external
triggers. The necessary science of truly multidimensional multicolor IR
spectroscopy is being developed in our laboratory. Experimental results are
compared to computer simulations to bring out atomic level understanding of the
processes in question.
Biomolecular structure determination and condensed matter dynamics. We
are applying multidimensional IR to the study of complex systems such as
peptides, proteins, liquids, membranes, and their composite interfaces.
Structural distributions, evolutions, and their environmental dependence are
investigated. Dynamics of vibrational relaxation, molecular reorientation, and
intermode vibrational energy transfer are studied. These processes are important
for the interpretation of multidimensional IR spectra. Strategic incorporation
of isotope labels and vibrational markers are used to zoom into atomic moieties
of particular interest.
Highlight of some recent projects
Onset of the 310-helical secondary structure:
Interplay between 310- and a-helices:
Conformations of a model terminally-blocked amino acid:
Funding supports from the following agencies are gratefully acknowledged:
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| CHE-0450045 | CRCC-37367 |
39148-G6 |
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