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Solvent mobility and the protein 'glass' transition
D Vitkup1, D Ringe, G A Petsko
1Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02454-9110, USA.
Nature Structural Biology
|January 14, 2000
Summary
Proteins transition to a glass-like state near 200 K, inhibiting function. Molecular dynamics simulations reveal solvent mobility is key to controlling protein atomic fluctuations, especially at higher temperatures.
Area of Science:
- Biophysics
- Structural Biology
- Computational Biology
Background:
- Proteins and biomolecules exhibit a dynamic transition to a glassy solid state around 200 K.
- This transition is characterized by reduced atomic fluctuations but can impair biological function.
Purpose of the Study:
- To elucidate the roles of solvent mobility and intrinsic protein energy landscapes in the dynamic transition.
- To understand the factors controlling protein atomic fluctuations and their impact on biological activity.
Main Methods:
- Utilized a novel molecular dynamics simulation technique.
- Simulated protein and solvent systems at varying temperatures to differentiate their contributions.
Main Results:
- Solvent mobility significantly influences atomic fluctuations above 180 K, acting as the dominant factor.
- Intrinsic protein properties become more critical in controlling fluctuations at temperatures below 180 K.
Conclusions:
- Solvent dynamics play a crucial role in regulating protein fluctuations essential for biological function.
- These findings complement experimental data, highlighting the indispensable role of the solvent environment.