To charge or not to charge?

Trends in Biotechnology

Volumn 19, Issue 4, 2001, Pages 132-135

  Sanchez Ruiz, Jose M ^a   Makhatadze, George I ^b  

^a UNIVERSITY OF GRANADA   (Spain)

^b PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; GENETIC ENGINEERING; MUTATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STABILITY; SURFACE PROPERTY; THERMOSTABILITY;

EID: 0035313828     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-7799(00)01548-1     Document Type: Review

References (31)

1. Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface
2. Increasing protein stability by altering long-range coulombic interactions
3. Rational modification of protein stability by the mutation of charged surface residues
4. Two exposed amino acid residues confer thermostability on a cold shock protein
5. Dominant forces in protein folding
6. Theory of protein titration curves. I. General equations for impenetrable spheres
7. Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability
8. Optimization of the electrostatic interactions in proteins of different functional and folding type
9. Electrostatic contributions to the stability of halophilic proteins
10. Electrostatic contributions to the stability of hyperthermophilic proteins
11. Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima
12. Single surface stabilizer
13. Surface electrostatic interactions contribute little of stability of barnase
14. Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability
15. Contributions of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structure in lambda repressor
16. Putative interhelix ion pairs involved in the stability of myoglobin
17. Charge-charge interactions influence the denatured state ensemble and contribute to protein stability
18. Calculation of the electric potential in the active site cleft due to alpha-helix dipoles
19. Energetics of charge-charge interactions in proteins
20. On the calculation of pKas in proteins
21. Intrinsic pKas of ionizable residues in proteins: An explicit solvent calculation for lysozyme
22. The determinants of pKas in proteins
23. Consistent calculations of pKas of ionizable residues in proteins: Semi-microscopic and microscopic approaches
24. Parameter dependence in continuum electrostatic calculations: A study using protein salt bridges
25. pKA values of carboxyl groups in the native and denatured states of barnase: The pKA values of the denatured state are on average 0.4 units lower than those of model compounds
26. Hydrogen bonds and the pH dependence of ovomucoid third domain stability
27. a values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions
28. pH dependence of stability of staphylococcal nuclease: Evidence of substantial electrostatic interactions in the denatured state
29. Realistic modeling of the denatured states of proteins allows accurate calculations of the pH dependence of protein stability
30. Does the elimination of ion pairs affect the thermal stability of cold shock protein from the hyperthermophilic bacterium Thermotoga maritima?
31. Contribution of surface salt bridges to protein stability