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Protein and Solvent Dynamics: How Strongly Are They Coupled?



G Caliskan, D Mechtani, J H. Roh, A Kisliuk, Alexei Sokolov, S Azzam, Marcus T. Cicerone, Sheng Lin-Gibson, I Peral


Analysis of Raman spectra of protein lysozyme demonstrates that its dynamics follow well the dynamics of solvents glycerol and trehalose. The protein s fast conformational fluctuations and low-frequency vibrations and their temperature variations are very sensitive to behavior of the solvents. Presented results provide an explanation for the counterintuitive observations reported earlier that protein relaxation is stronger in solid trehalose than in liquid glycerol. They also suggest an explanation as to why glycerol is so effective as a biological cryo-preservant.
Physical Review Letters


anhydrobiosis, drug delivery, dynamics, glass, light scattering, perservation, protein


Caliskan, G. , Mechtani, D. , Roh, J. , Kisliuk, A. , Sokolov, A. , Azzam, S. , Cicerone, M. , Lin-Gibson, S. and Peral, I. (2004), Protein and Solvent Dynamics: How Strongly Are They Coupled?, Physical Review Letters, [online], (Accessed April 21, 2024)
Created December 31, 2003, Updated October 12, 2021