Journal
PHYSICAL REVIEW LETTERS
Volume 101, Issue 13, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.101.135501
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Funding
- Department of Energy [DE-FG02-90ER45429]
- U. S. Department of Energy
- Office of Basic Energy Sciences [DE-AC0Z-06CH11357]
- CSGI
- MIUR
- EU
- U.S. Department of Energy (DOE) [DE-FG02-90ER45429] Funding Source: U.S. Department of Energy (DOE)
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Molecular dynamics simulations and neutron scattering experiments have shown that many hydrated globular proteins exhibit a universal dynamic transition at T-D = 220 K, below which the biological activity of a protein sharply diminishes. We studied the phononlike low-energy excitations of two structurally very different proteins, lysozyme and bovine serum albumin, using inelastic x-ray scattering above and below TD. We found that the excitation energies of the high-Q phonons show a marked softening above TD. This suggests that the large amplitude motions of wavelengths corresponding to this specific Q range are intimately correlated with the increase of biological activities of the proteins.
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