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Protein dynamics and stability: The distribution of atomic fluctuations in thermophilic and mesophilic dihydrofolate reductase derived using elastic incoherent neutron scattering

Journal Article


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Abstract


  • The temperature dependence of the dynamics of mesophilic and thermophilic dihydrofolate reductase is examined using elastic incoherent neutron scattering. It is demonstrated that the distribution of atomic displacement amplitudes can be derived from the elastic scattering data by assuming a (Weibull) functional form that resembles distributions seen in molecular dynamics simulations. The thermophilic enzyme has a significantly broader distribution than its mesophilic counterpart. Furthermore, although the rate of increase with temperature of the atomic mean-square displacements extracted from the dynamic structure factor is found to be comparable for both enzymes, the amplitudes are found to be slightly larger for the thermophilic enzyme. Therefore, these results imply that the thermophilic enzyme is the more flexible of the two.

UOW Authors


  •   Meinhold, L (external author)
  •   Clement, D (external author)
  •   Tehei, Moeava
  •   Daniel, R M (external author)
  •   Finney, J F (external author)
  •   Smith, J C (external author)

Publication Date


  • 2008

Citation


  • Meinhold, L., Clement, D., Tehei, M., Daniel, R., Finney, J. L. & Smith, J. C. (2008). Protein dynamics and stability: The distribution of atomic fluctuations in thermophilic and mesophilic dihydrofolate reductase derived using elastic incoherent neutron scattering. Biophysical Journal, 94 (12), 4812-4818.

Scopus Eid


  • 2-s2.0-45849083521

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=2801&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/1783

Has Global Citation Frequency


Number Of Pages


  • 6

Start Page


  • 4812

End Page


  • 4818

Volume


  • 94

Issue


  • 12

Place Of Publication


  • United States

Abstract


  • The temperature dependence of the dynamics of mesophilic and thermophilic dihydrofolate reductase is examined using elastic incoherent neutron scattering. It is demonstrated that the distribution of atomic displacement amplitudes can be derived from the elastic scattering data by assuming a (Weibull) functional form that resembles distributions seen in molecular dynamics simulations. The thermophilic enzyme has a significantly broader distribution than its mesophilic counterpart. Furthermore, although the rate of increase with temperature of the atomic mean-square displacements extracted from the dynamic structure factor is found to be comparable for both enzymes, the amplitudes are found to be slightly larger for the thermophilic enzyme. Therefore, these results imply that the thermophilic enzyme is the more flexible of the two.

UOW Authors


  •   Meinhold, L (external author)
  •   Clement, D (external author)
  •   Tehei, Moeava
  •   Daniel, R M (external author)
  •   Finney, J F (external author)
  •   Smith, J C (external author)

Publication Date


  • 2008

Citation


  • Meinhold, L., Clement, D., Tehei, M., Daniel, R., Finney, J. L. & Smith, J. C. (2008). Protein dynamics and stability: The distribution of atomic fluctuations in thermophilic and mesophilic dihydrofolate reductase derived using elastic incoherent neutron scattering. Biophysical Journal, 94 (12), 4812-4818.

Scopus Eid


  • 2-s2.0-45849083521

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=2801&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/1783

Has Global Citation Frequency


Number Of Pages


  • 6

Start Page


  • 4812

End Page


  • 4818

Volume


  • 94

Issue


  • 12

Place Of Publication


  • United States