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My name is Vijay Pande and
the lecture I'm going to present is on
studying "Protein Folding via Simulation".
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Just as protein folding itself, ie the act
of protein chain to assemble itself
into its final fold is of extreme
fundamental importance to biology,
since before any protein
can function must fold,
it's obvious that when
proteins fold incorrectly or
misfold that there could be natural,
drastic important biomedical implications.
And therefore it's perhaps not surprising
that there are many diseases associated
with protein misfolding such as CJD or
Creutzfeldt-Jakob disease also
known as mad cow disease in cows,
Alzheimer's disease, Parkinson's disease,
and much many others.
And part of the rationale for studying
protein folding itself is also to be able
to better understand
protein folding diseases.
And this is a very challenging
problem because protein folding while
there are many aspects that can
be understood experimentally,
there's still a whole wealth of details
that are just too difficult to examine
experimentally due to either the various
small sizes or fast timescales involved.
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It's also intriguing that not just
must proteins fold correctly, but
they often must fold in
a reasonable timescale.
A very nice example comes
from the p53 protein.
p53 is a protein and
very much important to cancer.
Roughly half of all known cancers
have a mutation involved in p53.
And there is recent evidence from various
experimental groups that suggests that p53
folds cotranslationally on the ribosome
actually forms dimers on the ribosome.
And it's natural to think that this
dimerization process would be kinetically
limited by translation and if this
dimerization doesn't occur on a relatively
fast rate that there
themselves could be problems.
So therefore it's perhaps intriguing to
think that protein folding must occur and
it must occur in some reasonably
chemically speedy process.
And this also becomes an interesting and
challenging problem to try to understand.
