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0:00
I'm Ivan Campeotto,
assistant professor in
microbial biotechnology
at the University of Nottingham,
and today, I will give
you an overview of
a key process in microbiology
called protein folding.
0:15
This lecture aims to
introduce protein
architectures to you,
discuss the driving forces
leading to protein folding,
explain the folding problem on
the computational and
conceptual point of use,
and discuss the folding problem
and the ways to solve it
both computationally
and experimentally.
0:35
There are several levels
of protein structure.
The primary structure
on the top left is
the simple composition of
amino acids of a protein.
In this example, in the
single-letter code,
A for alanine and so on,
K for lysine, valine,
W for tryptophan, Y for
tyrosine, H for histidine.
And this primary structure
already contains
all the chemical and
physical properties
that dictate further
levels of organization.
But there is no function yet.
The second level
of organization is
the secondary structure
in which the primary
structure adopts
secondary structure
elements, like here in
orange β strands in these arrows
or a helical form
called an alpha helix.
These secondary
structure elements come
further together to form
a tertiary structure.
This is the structure
or organization
which leads to function and
is essential for function.
Some proteins also have a
quaternary structure where
tertiary structure elements
come together, in this case
four of them, and have another
level of organization.
They can be independent
in their own function,
or they can affect
each other's function,
like in the case of hemoglobin
in a process, for instance,
called cooperativity.
