Electrostatic contribution of surface charge residues to the stability of a thermophilic protein: benchmarking experimental and predicted pKa values. [electronic resource]
Producer: 20120709Description: e30296 p. digitalISSN:- 1932-6203
- Archaeal Proteins -- chemistry
- Aspartic Acid -- chemistry
- Benchmarking
- Computational Biology -- methods
- Crystallography, X-Ray
- Glutamic Acid -- chemistry
- Hot Temperature
- Hydrogen-Ion Concentration
- Models, Molecular
- Mutation
- Protein Folding
- Protein Stability
- Protein Unfolding
- Ribosomal Proteins -- chemistry
- Static Electricity
- Surface Properties
- Thermococcus -- genetics
- Thermodynamics
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
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