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Related Concept Videos

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Updated: May 27, 2026

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method
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Mössbauer effect in proteins.

Robert D Young1, Hans Frauenfelder, Paul W Fenimore

  • 1Department of Physics, Arizona State University, P.O. Box 871504, Tempe, Arizona 85287-1504, USA.

Physical Review Letters
|November 24, 2011
PubMed
Summary
This summary is machine-generated.

A controversial "dynamical transition" in proteins is not required to explain experimental data. Fluctuations in the protein hydration shell, not internal protein motion, cause observed effects, simplifying protein dynamics analysis.

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Area of Science:

  • Biophysics
  • Protein Dynamics
  • Spectroscopy

Background:

  • Mössbauer effect and neutron scattering reveal increased protein displacement above 180 K.
  • This phenomenon, termed the 'dynamical transition,' is debated in scientific literature.

Purpose of the Study:

  • To propose a new interpretation of the Mössbauer effect in proteins.
  • To demonstrate that the 'dynamical transition' is not necessary to explain experimental observations.

Main Methods:

  • Analysis of Mössbauer spectroscopy data in proteins.
  • Investigating protein hydration shell fluctuations.
  • Utilizing dielectric spectrum analysis.

Main Results:

  • The observed increase in mean-square displacement and broad spectral lines are attributed to hydration shell fluctuations.
  • A new interpretation of Mössbauer spectra in proteins is presented.
  • The study shows no 'dynamical transition' is required.

Conclusions:

  • Protein hydration shell dynamics, not internal protein motion, explain the observed spectral broadening and displacement increase.
  • The proposed model simplifies the understanding of protein dynamics and spectral analysis.
  • Further research can validate this interpretation across various protein systems.