참고문헌
- Loladze, V. V., Ibarra-Molero, B., Sanchez-Ru, L. M. and Makhatadze, G. I. (1999) Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry 38, 16419-16423. https://doi.org/10.1021/bi992271w
- Akk, M. and Forsen, S. (1990) Protein stability and electrostatic interactions between solvent-exposed charged side chains. Proteins 8, 23-29. https://doi.org/10.1002/prot.340080106
- Roca, M., Messer, B. and Warshel, A. (2007) Electrostatic contributions to protein stability and folding energy. FEBS Lett. 581, 2065-2071. https://doi.org/10.1016/j.febslet.2007.04.025
- Garcia-Mira, M. M. and Schmid, F. X. (2006) Key role of coulombic interactions for the folding transition state of the Cold Shock Protein. J. Mol. Biol. 364, 458-468. https://doi.org/10.1016/j.jmb.2006.08.071
- Lindman, S., Xue, W., Szczepankiewicz, O., Bauer, M. C., Nilsson, H. and Lins, S. (2006) Salting the charged surface: pH and salt dependence of protein G B1 stability. Biophys. J. 90, 2911-2921. https://doi.org/10.1529/biophysj.105.071050
- Loladze, V. V. and Makhtadze, G. I. (2002) Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable. Protein Sci. 11, 147-177. https://doi.org/10.1110/ps.ps.27702
- Hendsch, Z. and Tidor, B. (1994) Do salt bridges stabilize proteins? A Continuum electrostatic analysis. Protein Sci. 3, 211-226.
-
Katherine, L. G. (2005) Eliminating positively charged lysine
${\varepsilon}-NH^{3+}$ Groups on the surface of carbonic anhydrase has no significant influence on its folding from Sodium Dodecyl Sulfate. J. Am. Chem. Soc. 127, 4707- 4714. https://doi.org/10.1021/ja043804d - Branchini, B. R., Southworth, T. L., Murtiashaw, M. H., Magyar, R. A., Gonzalez, S. A., Ruggiero, M. C. and Stroh, J. G. (2004) An Alternative Mechanism of Bioluminescence Color Determination in firefly luciferase. Biochemistry 43, 7255-7262. https://doi.org/10.1021/bi036175d
- Tafreshi, N., Sadeghizadeh, M., Emamzadeh, R., Ranjbar, B., Naderi-Manesh, H. and Hosseinkhani, S. (2008) sitedirected mutagenesis of firefly luciferase: Implication of conserved residue(s) in bioluminescence emission among firefly luciferases. Biochem. J. 412, 27-33. https://doi.org/10.1042/BJ20070733
- Alipour, B. S., Hosseinkhani, S., Nikkhah, M., Naderi-Manesh, H., Chaichi, M. J. and Osaloo, S. K. (2004) Molecular cloning, sequence analysis, and expression of a cDNA encoding the luciferase from the glow-worm Lampyris turkestanicus. Biochem. Biophys. Res. Commun. 325, 215-222. https://doi.org/10.1016/j.bbrc.2004.10.022
-
Tafreshi, N., Hosseinkhani, S., Sadeghizadeh, M., Sadeghi, M., Ranjbar, B. and Naderi-Manesh, H. (2007) The Influence of Insertion of a Critical Residue (
$Arg^{356}$ ) in Structure and Bioluminescence Spectra of Firefly Luciferase. J. Biol. Chem. 282, 8641-8647. https://doi.org/10.1074/jbc.M609271200 - Moradi, A., Hosseinkhani, S., Naderi-Manesh, H., Sadeghizadeh, M. and Alipour, B. S. (2009) Effect of charge distribution in a flexible loop on the bioluminescence color of Firefly luciferases. Biochemistry 48, 575-582. https://doi.org/10.1021/bi802057w
- Alipour, B. S., Hosseinkhani, S., Ardestani, S. K. and Moradi, A. (2009) the effective role of positive charge saturation in bioluminescence color and thermostability of firefly Luciferase. Photochem. Photobiol. Sci. 8, 847-855. https://doi.org/10.1039/b901938c
- Arnold, K., Bordoli, L., Kopp, J. and Schwede, T. (2006) The Swiss-Model Workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201. https://doi.org/10.1093/bioinformatics/bti770
- Schwede, T., Kopp, J., Guex, N. and Peitsch, M. C. (2003) Swiss-Model: an automated protein homology-modeling server. Nucleic. Acids. Res. 31, 3381-3385. https://doi.org/10.1093/nar/gkg520
- Guex, N. and Peitsch, M. C. (1997) Swiss-Model and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis 18, 2714-2723. https://doi.org/10.1002/elps.1150181505
- Conti, E., Franks, N. P. and Brick, P. (1996) Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4, 287-298. https://doi.org/10.1016/S0969-2126(96)00033-0
- Myers, J. K., Pace, C. N. and Scholtz, M. (1995) Denaturant m-values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148. https://doi.org/10.1002/pro.5560041020
- Roder, H. and Colon, W. (1997) Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7, 15-28. https://doi.org/10.1016/S0959-440X(97)80004-8
- Fersht, A. R., Matoushek, A. and Serrano, L. (1992) The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224, 771-783. https://doi.org/10.1016/0022-2836(92)90561-W
- Privalov, P. L. and Gill, S. J. (1988) Stability of protein structure and hydrophobic interaction. Adv. Protein. Chem. 39, 191-263. https://doi.org/10.1016/S0065-3233(08)60377-0
- Privalov, P. L. and Gill, S. J. (1989) The Hydrophobic Effect, a Reappraisal. Pure Appl. Chem. 61, 1907-1104.
- Kuntz, I. D. (1971) Hydration of macromolecules. III Hydration of polypeptides. J. Am. Chem. Soc. 93, 514-516. https://doi.org/10.1021/ja00731a036
- Chiti, F., Stefani, M., Taddei, N., Ramponi, G. and Dobson, C. M. (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424, 805-808. https://doi.org/10.1038/nature01891
- Pace, C. N. (1975) The stability of globular proteins. CRC Crit. Rev. Biochem. 3, 1-43. https://doi.org/10.3109/10409237509102551
- Pace, C. N. (1986) Determination and analysis of Urea and Guanidium Curves. Methods Enzymol. 131, 266-279. https://doi.org/10.1016/0076-6879(86)31045-0
- Zarrine-Afsar, A. and Davidson, A. R. (2004) The analysis of protein folding kinetic data produced in protein engineering experiments. Methods 34, 41-50. https://doi.org/10.1016/j.ymeth.2004.03.013
- Eyring, H. (1935) the activated complex and the absolute rate of chemical reactions. Chem. Rev. 17, 65-77. https://doi.org/10.1021/cr60056a006
- Fersht, A. R., Matoushek, A., Bycroft, M., Kellis, J. T. and Serrano, L. (1991) Physical-organic molecular biology: pathway and stability of protein folding. Pure Appl. Chem. 63, 187-194. https://doi.org/10.1351/pac199163020187
피인용 문헌
- Kinetic and thermodynamic properties of pseudomonas fluorescence lipase upon addition of proline vol.55, 2013, https://doi.org/10.1016/j.ijbiomac.2012.12.046
- Variant of the Thermomyces lanuginosus lipase with improved kinetic stability: A candidate for enzyme replacement therapy vol.172, 2013, https://doi.org/10.1016/j.bpc.2012.12.003
- The Effect of Surface Charge Saturation on Heat-induced Aggregation of Firefly Luciferase vol.91, pp.5, 2015, https://doi.org/10.1111/php.12467
- Design of thermostable luciferases through arginine saturation in solvent-exposed loops vol.24, pp.12, 2011, https://doi.org/10.1093/protein/gzr051
- Implication of Arg213 and Arg337 on the kinetic and structural stability of firefly luciferase vol.52, 2013, https://doi.org/10.1016/j.ijbiomac.2012.09.007
- Step-wise addition of disulfide bridge in firefly luciferase controls color shift through a flexible loop: a thermodynamic perspective vol.12, pp.2, 2013, https://doi.org/10.1039/C2PP25140J
- The role of trehalose for metastable state and functional form of recombinant interferon beta-1b vol.163, pp.3, 2013, https://doi.org/10.1016/j.jbiotec.2012.11.010
- firefly luciferases identified by surveying consecutive single amino acid deletion mutations in a thermostable variant vol.115, pp.1, 2017, https://doi.org/10.1002/bit.26451