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Effects of
Strutural Stability on the Adsorption of Bacteriophage T4
Lysozyme
Johan Fröberg: Physical
Chemistry, Dept. of Chemistry, KTH
I am doing my graduate work in the Surface Force Group which
is a
cooperation between the dept of Physical Chemistry at KTH, and
the
Institute for Surface Chemistry both in Stockholm. Our main
experimental method is an interferometric technique which gives a
direct measure of the interaction between two solid surfaces as a
function of their separation with Angstrom resolution.
The analysis is done within the framework of long-range forces
such as electrostatic
double layer repulsion and van der Waals attraction, as well as
steric
or structural forces, due interaction between adsorbed layers,
and
hydrophobic interactions.
My objective is to study how the adsorption of
biomolecules, mainly proteins, alters the observed interactions.
The
direct measure of the separation, with a known zero contact
between
bare surfaces, also make an analysis of the structure of the
adsorbed
layer possible. Different proteins and different properties of
the
protein give a wide variety of effects. Among the more important
seem
the structural stability to be. My last study therefore concerns
a
wild type protein and one synthetic variant differing in
structural
stability, which allow us to study the importance of different
folding
energies.
In order to complement I have also used other surface
sensitive techniques, e.g., ellipsometry, and written some
programs
for the theoretical analysis fo the results.
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