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Water around thermophilic proteins: the role of charged and apolar atoms
- Source :
- Journal of physics. Condensed matter : an Institute of Physics journal. 22(28)
- Publication Year :
- 2011
-
Abstract
- The thermal response of three proteins with mesophilic, thermophilic and hyperthermophilic character hints at the essential role played in thermostability by the protein-water interface. The formation of spanning water clusters enveloping the macromolecule and their resistance to thermal stress is shown to correlate with the charge distribution at the protein surface; in particular our findings suggest an effective role of the superficial charge distribution in stabilizing the global connectivity of the hydration water.
- Subjects :
- Models, Molecular
Protein Folding
Hot Temperature
Protein Conformation
Surface Properties
Static Electricity
Sequences
Phase Transition
General Materials Science
Thermal stability
Computer Simulation
Thermostability
Behavior
Binding Sites
Chemistry
Hydrogen bond
Thermophile
Temperature
Charge density
Proteins
Water
Classification
Condensed Matter Physics
Hyperthermophile
Enzymes
Surfaces
Solutions
Biochemistry
Models, Chemical
Chemical physics
Hyperthermophiles
Flexibility
Stability
Mesophile
Macromolecule
Protein Binding
Subjects
Details
- ISSN :
- 1361648X
- Volume :
- 22
- Issue :
- 28
- Database :
- OpenAIRE
- Journal :
- Journal of physics. Condensed matter : an Institute of Physics journal
- Accession number :
- edsair.doi.dedup.....a96f535594183bf40f12408048381ce0