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.
Studies of phononlike low-energy excitations of protein molecules by inelastic X-ray scattering / D. Liu; X. Q. Chu; M. Lagi; Y. Zhang; E. Fratini; P. Baglioni; A. Alatas; A. Said; E. Alp; S. H. Chen. - In: PHYSICAL REVIEW LETTERS. - ISSN 0031-9007. - STAMPA. - 101:(2008), pp. 135501-1-135501-4. [10.1103/PhysRevLett.101.135501]
Studies of phononlike low-energy excitations of protein molecules by inelastic X-ray scattering
LAGI, MARCO;FRATINI, EMILIANO;BAGLIONI, PIERO;
2008
Abstract
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.File | Dimensione | Formato | |
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