The cold denaturation of proteins

A study the cold denaturation of proteins by means of physical methods as neutron scattering experiments, calorimetry, densitometry and others. Internship at the Institute Laue Langevin.
Description of the internship
Proteins can denature when submitted to extreme conditions as high or low temperature or pressure. Denaturation by heat was studied in detail. Often it leads to aggregation and thus to irreversibility of the process. Much less is known about the cold denaturation, which seems to be largely reversible and must rely on different mechanisms. High hydrostatic pressure can shift the transition temperatures and have additional protective or destabilizing effects.
We want now to investigate by means of different experimental techniques as calorimetry, FT-IR, densitometry and neutron scattering the impact of cold denaturation on the structure and dynamics of proteins and develop a new theoretical model to describe the transition. These effects have to be related to the functionality of the biological systems. Our findings can provide important input for biotechnology or medical applications.
Qualifications of the applicant
This two-year research project is dedicated to a students following the SoftNano Program of the UGA Graduate School, in the Soft Matter and Biophysics 1st-year.
Expected skills: background in thermodynamics, biophysics
 
Publications
S. A. Hawley, Biochemistry, 1971, 10, 2436–2442.
L. Smeller, Biochim Biophys Acta, 2002, 1595, 11-29.
J. Peters, J. Marion, F. J. Becher, M. Trapp, T. Gutberlet, D. J. Bicout and T. Heimburg, Sci Rep, 2017, 7, 15339

 
Published on February 12, 2021
Updated on September 19, 2023