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Protein Biophysics Group - Introduction

The phenomenon of protein aggregation, which used to be associated with the banality of spoilt protein samples, has recently become a major puzzle in bioscience. In part, this happened due to the realization that orderly-aggregated proteins - amyloids - constitute the molecular basis of several neurodegenerative diseases (to mention only the most attention-receiving Alzheimer Disease and Creutzfeldt-Jakob Disease – the “prion” disease).

Then, another puzzle: Does the native conformational state of a protein correspond to its global energy minimum, or rather it is only a biologically-functional structure transiently trapped in a local energy minimum, but perhaps – in a timescale longer than the lifespan of the longest living creatures – doomed to reach the deeper global minimum through... aggregation?

There is, however, at least one more equally compelling reason to study mechanisms of protein aggregation. Namely, if amino acid sequences of a polypeptide chain were drawn at random, then only a decisive minority of such incidental combinations could fold into stable proteins, while the overwhelming reminder yield aggregates and unstructured coils. Once a protein loses this peculiar degree of structural stability, as it happens in the “molten globule” state, it becomes prone to aggregation. One could hypothesize, somewhat provocatively, that the dull regularity and abundance of biologically functional structures of the dozens of thousands of proteins appears to include none but physico-statistical peculiarities.

This is our main rationale of this quest for a comprehensive view on mechanisms of protein aggregation, which may give important molecular clues, as to the medical strategies of preventing and curing protein aggregation-associated diseases.

In collaboration with our research partners, we use a variety of physicochemical methods, including infrared spectroscopy, high-pressure techniques, circular dichroism, pressure perturbation calorimetry, etc.