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 their mean-squared atomic displacements r2 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 approximately 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 r2 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.
Khodadadi
S
S
Department of Polymer Science, The University of Akron, Akron, Ohio 44325, USA.
Pawlus
S
S
Roh
J H
JH
Garcia Sakai
V
V
Mamontov
E
E
Sokolov
A P
AP
D001703:Biophysics / Q000379:methods; D002627:Chemistry, Physical / Q000379:methods; D004247:DNA / Q000737:chemistry; D015233:Models, Statistical; D008968:Molecular Conformation; D009113:Muramidase / Q000737:chemistry; D009502:Neutrons; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012313:RNA / Q000737:chemistry; D012542:Scattering, Radiation; D013696:Temperature; D014867:Water / Q000737:chemistry
D011506:Proteins; D014867:Water; D012313:RNA; D004247:DNA; D009113:Muramidase