The origin of the dynamic transition in proteins
Despite extensive efforts in experimental and computational studies, the microscopic understanding of dynamics of biological macromolecules remains a great challenge. It is known that hydrated proteins, DNA and RNA, exhibit a so-called "dynamic transition." It appears as a sharp rise of th...
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Veröffentlicht in: | The Journal of chemical physics 2008-05, Vol.128 (19), p.195106-195106-5 |
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Sprache: | eng |
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Zusammenfassung: | Despite extensive efforts in experimental and computational studies, the microscopic understanding of dynamics of biological macromolecules remains a great challenge. It is known that hydrated proteins, DNA and RNA, exhibit a so-called "dynamic transition." It appears as a sharp rise of their mean-squared atomic displacements
⟨
r
2
⟩
at temperatures above
200
-
230
K
. Even after a long history of studies, this sudden activation of biomolecular dynamics remains a puzzle and many contradicting models have been proposed. By combining neutron and dielectric spectroscopy data, we were able to follow protein dynamics over an extremely broad frequency range. Our results show that there is no sudden change in the dynamics of the protein at temperatures around
∼
200
-
230
K
. The protein's relaxation time exhibits a smooth temperature variation over the temperature range of
180
-
300
K
. Thus the experimentally observed sharp rise in
⟨
r
2
⟩
is just a result of the protein's structural relaxation reaching the limit of the experimental frequency window. The microscopic mechanism of the protein's structural relaxation remains unclear. |
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ISSN: | 0021-9606 1089-7690 |
DOI: | 10.1063/1.2927871 |