Water Determines the Structure and Dynamics of Proteins
CEA Paris-Saclay · Commissariat à l'Énergie Atomique et aux Énergies Alternatives · +12 more institutions
Abstract
Water is an essential participant in the stability, structure, dynamics, and function of proteins and other biomolecules. Thermodynamically, changes in the aqueous environment affect the stability of biomolecules. Structurally, water participates chemically in the catalytic function of proteins and nucleic acids and physically in the collapse of the protein chain during folding through hydrophobic collapse and mediates binding through the hydrogen bond in complex formation. Water is a partner that slaves the dynamics of proteins, and water interaction with proteins affect their dynamics. Here we provide a review of the experimental and computational advances over the past decade in understanding the role of…
Citation impact
- FWCI
- 42.82
- Percentile
- 100%
- References
- 314
Authors
9- MBMarie‐Claire Bellissent‐FunelCorresponding
CEA Paris-Saclay, Commissariat à l'Énergie Atomique et aux Énergies Alternatives, Centre National de la Recherche Scientifique, Laboratoire Léon Brillouin
- AHAli Hassanali
The Abdus Salam International Centre for Theoretical Physics (ICTP)
- MHMartina Havenith
Ruhr University Bochum
- RHRichard H. Henchman
University of Manchester
- PPPeter Pohl
Johannes Kepler University of Linz
Topics & keywords
- Chemistry
- Biomolecule
- Molecular dynamics
- Protein dynamics
- Chemical physics
- Neutron spectroscopy
- Folding (DSP implementation)
- Hydrogen bond
- Clean water and sanitation
Funding
- RSRoyal Swedish Academy of Sciences
- ASAustrian Science FundAward: P23679
- VVetenskapsrådet
- BABiotechnology and Biological Sciences Research CouncilAward: BB/K001558/1
- EREuropean Research CouncilAward: 258748
- DODivision of Molecular and Cellular BiosciencesAward: MCB-1050966
- LDLaboratory Directed Research and Development