Hello, my name is Vladimir Uversky.
I'm an associate professor in
the Department of Molecular Medicine in the University of South Florida.
I will talk today about the roles of intrinsic disorder in protein interaction networks.
Here is an outline of my talk.
First, I will introduce the intrinsically disordered proteins.
Then I will talk about their structural properties and some sequence features.
Then I will discuss the abundance and functions of the intrinsically disordered proteins.
Then I will talk about the role of
intrinsic disorder in protein-protein interaction networks,
and will try to answer the question of why these proteins are
commonly found in protein-protein interaction networks.
I will conclude with some remarks and an acknowledgment.
Before going into the detail of my talk, a brief introduction
to the protein intrinsic disorder concept is needed.
According to the classical structure-to-function paradigm,
all the information for a protein to be functional
is encoded in its unique three-dimensional structure, and
information about this structure is encoded in its unique amino acid sequence.
There are two general models which support this idea:
the 'lock-and-key' model, and the 'induced-fit' model.
The protein-structure function paradigm is a very useful idea which can be
considered as the 'Big Bang' that created the entire universe of modern protein science.
This slide shows that all branches of protein science originated from this idea.
The classical structure-to-function paradigm works for many proteins,
but not for every protein,
and quite a few exceptions to this rule were discovered over the years.