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Folding of peptides and proteins
Protein folding, the process by which a protein assumes its
three-dimensional shape, is one of the basic unsolved problems of
biophysical and biochemical research. The structural changes taking
place during protein folding, especially during the early stages, are
as yet very poorly understood. This is because high-resolution
structural techniques generally lack the time resolution necessary for
observation of folding dynamics, whereas methods that have the
required time resolution generally
lack structural specificity. We use
two-dimensional optical spectroscopy in combination with site-specific
isotope labeling to study folding in real time.
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The folding is triggered with
an external stimulus, and the
conformation is probed in real time using 2D-IR
at a series of time
delays with respect
to the trigger.
This will make it possible to
obtain a structurally and
temporally resolved picture of
protein folding, which can be
regarded as a 'molecular movie' of
the folding process. The combined
spatial and temporal resolution of
the proposed method is far beyond
that of conventional methods, and will
allow us to address research
problems that have as yet been
difficult to investigate.
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