Amino Acid Contribution to Protein Solubility: Asp, Glu, and Ser Contribute more Favorably than the other Hydrophilic Amino Acids in RNase Sa
- 16 February 2007
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 366 (2), 449-460
- https://doi.org/10.1016/j.jmb.2006.10.026
Abstract
No abstract availableKeywords
This publication has 68 references indexed in Scilit:
- pK values of the ionizable groups of proteinsProtein Science, 2006
- Decrease in Protein Solubility and Cataract Formation Caused by the Pro23 to Thr Mutation in Human γD-Crystallin,Biochemistry, 2005
- The P23T Cataract Mutation Causes Loss of Solubility of Folded γD-CrystallinJournal of Molecular Biology, 2004
- The Structure of Aqueous Guanidinium Chloride SolutionsJournal of the American Chemical Society, 2004
- Charge–Charge Interactions are Key Determinants of the pK Values of Ionizable Groups in Ribonuclease Sa (pI=3.5) and a Basic Variant (pI=10.2)Journal of Molecular Biology, 2003
- The effect of net charge on the solubility, activity, and stability of ribonuclease SaProtein Science, 2001
- Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3Journal of Molecular Biology, 1998
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- Studies on engineering crystallizability by mutation of surface residues of human thymidylate synthaseJournal of Crystal Growth, 1992
- Variation of lysozyme solubility as a function of temperature in the presence of organic and inorganic saltsJournal of Crystal Growth, 1992