ArticleScientific reports2018
The effects of pressure on the energy landscape of proteins.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- High-pressure single-crystal diffraction at the Australian Synchrotron.Journal of synchrotron radiation · 2023Article
- Unravelling the Adaptation Mechanisms to High Pressure in Proteins.International journal of molecular sciences · 2022Article
- Mesophilic Pyrophosphatase Function at High Temperature: A Molecular Dynamics Simulation Study.Biophysical journal · 2020Article
- Universality and Structural Implications of the Boson Peak in Proteins.Biophysical journal · 2019Article
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4 authors.
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Abstract
Protein dynamics is characterized by fluctuations among different conformational substates, i.e. the different minima of their energy landscape. At temperatures above ~200 K, these fluctuations lead to a steep increase in the thermal dependence of all dynamical properties, phenomenon known as Protein Dynamical Transition. In spite of the intense studies, little is known about the effects of pressure on these processes, investigated mostly near room temperature. We studied by neutron scattering the dynamics of myoglobin in a wide temperature and pressure range. Our results show that high pressure reduces protein motions, but does not affect the onset temperature for the Protein Dynamical Transition, indicating that the energy differences and barriers among conformational substates do not change with pressure. Instead, high pressure values strongly reduce the average structural differences between the accessible conformational substates, thus increasing the roughness of the free energy landscape of the system.
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