This talk deals with the mechanisms of protein folding reactions.
The outline of my talk,
I will first give a brief introduction into the history of protein folding,
I will then talk about intrinsically slow reactions coupled to protein folding.
These are prolyl peptide bond isomerization,
non-prolyl peptide bond isomerization,
association reactions of oligomeric proteins.
In the second part of my talk,
I will address kinetic mechanisms of protein folding,
and I will specifically discuss how we can
place an intermediate on a kinetic folding pathway.
This will be shown in two case studies.
The first one is folding of Iysozyme,
and the second one is folding of Semliki Forest virus protease.
If you regard protein folding as a chemical reaction,
we start from the ensemble of different conformations representing
the unfolding state and end up in the biologically active native state,
which represents a single conformation with defined side chain and backbone interactions.
This is a simplification, of course,
because we know that there is conformation of fluctuations in the native state.
But the basic problem in protein folding is how the ensemble of
different states from the unfolded ensemble reach the native state.
And the questions we are addressing is,
are there intermediates located between the unfolded and the native state and what are
the rate limiting steps between the unfolded and the native state?
My talk deals with protein folding studies in vitro,