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Water Determines the Structure and Dynamics of Proteins
Marie-Claire Bellissent-Funel1, Ali Hassanali2, Martina Havenith3
1Laboratoire Léon Brillouin (CEA-CNRS) CEA Saclay F-91191 Gif Sur Yvette, France.
Chemical Reviews
|May 18, 2016
Summary
Water is crucial for protein stability, structure, dynamics, and function. Recent advances in experimental and computational methods reveal water's vital role in protein dynamics and function.
Area of Science:
- Biochemistry and Molecular Biology
- Structural Biology
- Biophysics
Background:
- Water is essential for biomolecular stability, structure, dynamics, and function.
- The aqueous environment significantly impacts biomolecular stability and interactions.
- Water plays direct roles in protein catalysis, folding, and complex formation.
Purpose of the Study:
- To review experimental and computational advances in understanding water's role in protein dynamics, structure, and function over the past decade.
- To highlight how water assists proteins in their biological roles.
- To synthesize current knowledge on water-protein interactions.
Main Methods:
- X-ray and neutron crystallography
- Nuclear Magnetic Resonance (NMR) spectroscopy
- Terahertz spectroscopy
- Mass spectrometry
- Thermodynamics
- Computer simulations
Main Results:
- Water participates chemically in protein and nucleic acid catalysis.
- Water mediates protein folding via hydrophobic collapse and complex formation through hydrogen bonds.
- Water dynamics are intrinsically linked to protein dynamics.
Conclusions:
- A decade of research, combining advanced experimental and computational techniques, has deepened our understanding of water's role in protein science.
- Future advances in simulations and experimental sensitivity will further elucidate water's protagonist role in protein dynamics and function.
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