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Vesa Hytönen - Protein Dynamics

About research group

Proteins adapt conformationally to their environment in response to chemical and physical signals arising from interactions with other molecules, and as a result of chemical modifications. Therefore, conformational changes in proteins are often essential for the protein function. The Protein Dynamics Group uses experimental and computational methods to elucidate the relation between protein conformation and function.

We study structural dynamics of the proteins in cellular adhesion sites called focal adhesions. In particular, we try to understand the mechanisms behind cellular mechanosensing. These studies involve cellular models, tailored hydrogel substrates for cell adhesion studies, protein engineering and molecular dynamics simulations. We collaborate in this project with University of Geneva.

Another approach to understand the impact of environment on protein conformation is a project where we study the effects of electric fields on protein structure and function. This research is performed in collaboration with University of Jyväskylä and Technical University of Tampere.

We utilize a broad set of biophysical characterization methods in our research, including calorimetry, biosensors and spectroscopic methods. Recombinant proteins and protein engineering are in routine use, and this expertise is utilized in research aiming for biofunctionalized materials, focusing on nanocellulose and various metals. In this field, we collaborate with VTT Espoo, University of Jyväskylä and Technical University of Tampere.

Our research group is also involved in projects developing novel diagnostic tools and vaccines. This work has a main focus on viruses, with the recently launched THERDIAB-project aiming to develop novel molecular tools to fight against enteroviral diseases and type 1 diabetes. This project is performed in collaboration with Karolinska Institutet.

Recent results

 Reversibly biotin-binding avidin mutant Switchavidin

The chicken avidin mutant Switchavidin was designed to display reversible high affinity binding to biotin. This was accomplished by mutating an amino acid in the biotin-binding site and another amino acid in the subunit interface. In addition, introducing neutralizing mutations on the protein surface reduced non-specific binding of macromolecules.

Taskinen et al.
Switchavidin: reversible biotin-avidin-biotin bridges with high affinity and specificity.
Bioconjug Chem 2014 ;25(12)2233-43

 Investigation of talin-integrin pair under mechanical load

 Talin is a key player in the complex network of force-bearing structures in adhesion sites. In this paper, we studied the stability of integrin-talin complexes by subjecting the complexes to mechanical force in a set of steered molecular dynamics simulations.

Kukkurainen et al.
The talin-integrin interface under mechanical stress.
Mol Biosyst 2014 ;10(12)3217-28

 Understanding the regulation of cellular adhesion

 Talin-integrin interaction is essential link within the cellular machinery connecting cell and its environment. By using engineered integrin forms with increased affinity to talin, it was possible to tailor the substrate sensing of fibroblast cells.

Pinon et al.
Talin-bound NPLY motif recruits integrin-signaling adapters to regulate cell spreading and mechanosensing.
J Cell Biol 2014 ;205(2)265-81


 Novel biosensor methods

 Electrolyte-gated organic field-effect transistors are successfully used as biosensors to detect binding events occurring at distances from the transistor electronic channel that are much larger than the Debye length in highly concentrated solutions. A successful proof-of-principle of their use as sensors directly in serum is provided.

Palazzo et al.
Detection Beyond Debye's Length with an Electrolyte-Gated Organic Field-Effect Transistor.

Adv Mater. 2015 Feb;27(5):911-6.




Biocenter Finland plays important role in our operation and
we provide services in protein production and protein analysis

Biokatu 8, 12
33520 Tampere, Finland
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Last update: 13.3.2015 11.00 Muokkaa

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+358 3 355 111

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