Related Experiment Video
Updated: May 27, 2026

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method
Published on: July 19, 2019
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.
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.
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.
More Related Videos
08:48High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
12:47Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Related Concept Videos
Nuclear Overhauser Enhancement (NOE)
Proton (¹H) NMR: Chemical Shift
Absorption signals of all the protium nuclei in a...
Proteomics
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...