Protein Structure and Dynamics
Structures and molecular motions of proteins and their interactions with
other biologically relevant molecules are studied mostly by methods of
nuclear magnetic resonance. Application of standard NMR techniques to
interesting biological systems is combined with our own
Examples of proteins recently and currently studied in our laboratory are briefly reviewed below.
Mouse major urinary protein I (MUP-I) has been recently investigated in
our group as an example of a mammalian pheromone-binding protein.
Standard NMR techniques have been used to study structural details of
MUP-I in complex with a natural pheromone. NMR relaxation measurements
have been employed in mapping internal dynamics of free and
pheromone-bound MUP-I . Analysis of data obtained at various
temperatures was used to improve reliability of the measured values and
to obtain additional information about dynamical and thermodynamical
changes upon binding. The results have been compared to molecular dynamic
simulations [2,3]. Both NMR relaxation and MD simulations indicated that
the pheromone binding does not rigidify the MUP-I structure. On the
conrary, several regions of increased flexibility have been identified in
the protein-pheromone complex.
Chemosensory protein 1 (CSP1) of Bombyx mori is believed to bind
small hydrophobic, like MUP-I. In spite of the functional similarity
structures of CSP1 (and related insect proteins) differes from the
typical lipocalin fold of MUP-I. In collaboration with the Department of
Ecology at the Lund University, 3D structure of CSP1 has been solved in
our laboratory based on NMR data .
A protein putatively involved in molybdopterin synthesis has been studied
as target TA1019 of the Thermoplasma acidophillum structural
genomic project at the University of Toronto. Due to the low solubility
and limited stability, TA1019 has been excluded from the automated
protocol of structure determination. Based on data obtained at
experimentally challenging conditions, a structural model of TA1019 has
been built in our laboratory.
Other proteins which our group is interested in include mammalian
lectin-like receptor domains, plant lipid-transfer proteins, bacterial
RNA polymerases, retroviral proteases etc. Structural
investigations of these proteins are usually combined with binding
studies and various biological assays perfored in collaborating groups
(mostly at the institutes of the Czech Academy of Sciences). Our goal is
to provide a complex description of the systems and thus help to
understand their biological roles.
Design © oliver 2007