Nozomi Ando
Graduate Student

192 Clark Hall
Department of Physics, Cornell University
Ithaca, NY 14853-2501

tel : (607) 255-8678
fax : (607) 255-8751

email : nando @ bigbro.biophys.cornell.edu


Protein under Pressure: A Short Introduction

Humans have cooked meat and fish for hundreds of thousands of years. Methods include heating with fire, pickling in vinegar, and curing in brine. But it was only very recently, in 1914, when P. W. Bridgman accidentally discovered that pressurized egg white appeared cooked.

The important discovery was that pressure – like heat, pH, and salt – can unfold proteins.

Proteins, you may recall, are the molecules which carry out most of the functions necessary in life. A protein’s functions are determined by its specific folded conformation. Misfolded proteins can therefore have malignant functions, and there is a whole class of protein misfolding diseases which include Mad Cow and Alzheimer’s.

Why should we study high-pressure effects on proteins? There are many reasons, but to summarize… First, we should not forget that pressure is biologically relevant – life spans a large range of pressures, yet it is relatively unexplored. Secondly, the physics of protein pressure unfolding is not fully understood. Finally, protein folding is an important problem, and pressure is a tool to study this problem, which is both similar and complementary to other perturbants.

In our lab, we are interested in understanding the effects of pressure on biomacromolecules and using pressure to perturb protein structure in order to understand how molecular interactions relate to structure, how structure is related to function, and the mechanism of misfolding. The various techniques we use include: high-pressure crystallography, high-pressure solution small angle X-ray scattering and high-pressure fluorescence/absorption spectroscopy and static light scattering.