1469-896X/asset/olbannerleft.gif?v=1&s=d218899ae53b2862ab119790ed504b8d72122fb3)
1469-896X/asset/olbannerright.gif?v=1&s=59470eb9a1d9b7b13b1be75e9445e6c46ee2214f)
Article
You have full text access to this OnlineOpen article
Thermally denatured state determines refolding in lipase: Mutational analysis
Article first published online: 6 APR 2009
DOI: 10.1002/pro.126
Copyright © 2009 The Protein Society
Additional Information
How to Cite
Ahmad, S. and Rao, N. M. (2009), Thermally denatured state determines refolding in lipase: Mutational analysis. Protein Science, 18: 1183–1196. doi: 10.1002/pro.126
Publication History
- Issue published online: 26 MAY 2009
- Article first published online: 6 APR 2009
- Accepted manuscript online: 6 APR 2009 12:00AM EST
- Manuscript Accepted: 30 MAR 2009
- Manuscript Revised: 23 MAR 2009
- Manuscript Received: 26 FEB 2009
Funded by
- CSIR Junior Fellowship
- NIMTLI grant. Grant Number: #TLP005
References
- 1, , , ( 1996) Forces contributing to the conformational stability of proteins. FASEB J 10: 75–83.
- 2( 1996) The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J 10: 27–34.
- 3, , , ( 1996) Protein folding for realists: a timeless phenomenon. Protein Sci 5: 991–1000.Direct Link:
- 4, ( 2001) Some thermodynamic implications for the thermostability of proteins. Protein Sci 10: 1187–1194.Direct Link:
- 5( 2003) Protein folding and misfolding. Nature 426: 884–890.
- 6, ( 2006) Lessons in stability from thermophilic proteins. Protein Sci 15: 1569–1578.Direct Link:
- 7, ( 1991) Denatured states of proteins. Annu Rev Biochem 60: 795–825.
- 8, , , ( 1996) The concept of a random coil. Residual structure in peptides and denatured proteins. Fold Des 1: R95–R106.
- 9
- 10, ( 2007) Atomic-level characterization of disordered protein ensembles. Curr Opin Struct Biol 17: 3–14.
- 11( 2002) The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space. Adv Protein Chem 62: 1–23.
- 12, , , ( 2003) Role of residual structure in the unfolded state of a thermophilic protein. Proc Natl Acad Sci USA 100: 11345–11349.
- 13, ( 2008) Folding versus aggregation: polypeptide conformations on competing pathways. Arch Biochem Biophys 469: 100–117.
- 14, , ( 2000) Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Protein Sci 9: 1395–1398.Direct Link:
- 15, , ( 2004) Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state. J Mol Biol 338: 827–837.
- 16, ( 2005) Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. J Mol Biol 353: 174–185.
- 17, ( 2008) Advances in laboratory evolution of enzymes. Curr Opin Chem Biol 12: 151–158.
- 18, , ( 2008) Protein design by directed evolution. Annu Rev Biophys 37: 153–173.
- 19, ( 2009) Directed enzyme evolution: climbing fitness peaks one amino acid at a time. Curr Opin Chem Biol 13: 1–7.
- 20, , ( 2009) Shedding light on the efficacy of laboratory evolution based on iterative saturation mutagenesis. Mol Biosyst 5: 115–122.
- 21, ( 2009) Protein engineering handbook. Weinheim: Wiley-VCH.
- 22, ( 2000) Temperature adaptation of enzymes: lessons from laboratory evolution. Adv Protein Chem 55: 161–225.
- 23, ( 2001) How do thermophilic proteins deal with heat? Cell Mol Life Sci 58: 1216–1233.
- 24, , , ( 2005) Directed evolution of enzyme stability. Biomol Eng 22: 21–30.
- 25, , , ( 2004) Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase. J Mol Biol 341: 1271–1281.
- 26, , , ( 2008) Thermostable Bacillus subtilis lipases: in vitro evolution and structural insight. J Mol Biol 381: 324–340.
- 27, , . Mechanism of protein folding. In: CreightonED, Ed. ( 1998) Protein structure: a practical approach. Oxford: Oxford Press, pp 311–330.
- 28, ( 2000) The use of circular dichroism in the investigation of protein structure and function. Curr Protein Pept Sci 1: 349–384.
- 29, ( 2000) Folding and association of oligomeric and multimeric proteins. Adv Protein Chem 53: 329–401.
- 30, , ( 2008) Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 25: 1487–1499.
- 31, , , , ( 2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424: 805–808.
- 32, ( 2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333–366.
- 33, ( 2007) Intermediates: ubiquitous species on folding energy landscapes? Curr Opin Struct Biol 17: 30–37.
- 34, , ( 2008) Extensive formation of off-pathway species during folding of an alpha-beta parallel protein is due to docking of (non)native structure elements in unfolded molecules. J Am Chem Soc 130: 16914–16920.
- 35, , ( 1987) Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc Natl Acad Sci USA 84: 6663–6667.
- 36, ( 1990) Intermediates in the folding reactions of small proteins. Annu Rev Biochem 59: 631–660.
- 37, , , ( 1992) Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. Biochemistry 31: 1464–1476.
- 38, ( 2003) Proline can have opposite effects on fast and slow protein folding phases. Biophys J 85: 1215–1222.
- 39( 1993) Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. Annu Rev Biophys Biomol Struct 22: 123–142.
- 40, ( 1998) The stability of proteins in extreme environments. Curr Opin Struct Biol 8: 738–748.
- 41, , , , , ( 2008) Structural analysis of a β-helical protein motif stabilized by targeted replacements with conformationally constrained amino acids. J Phys Chem B 112: 13101–13115.
- 42, , , ( 2008) Conformational preferences of β- and γ-aminated proline analogues. J Phys Chem B 112: 14045–14055.
- 43, , , , , ( 2008) Conformational preferences of alpha-substituted proline analogues. J Org Chem 73: 3418–3427.
- 44, , , ( 2005) Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa. Protein Sci 14: 1934–1938.Direct Link:
- 45, ( 2006) Electrostatic interactions in the denatured state and in the transition state for protein folding: effects of denatured state interactions on the analysis of transition state structure. J Mol Biol 359: 1437–1446.
- 46, , ( 2006) Iterative saturation mutagenesis on the basis of B factors as a strategy for increasing protein thermostability. Angew Chem Int Ed Engl 45: 7745–7751.Direct Link:
- 47, ( 2007) Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes. Nat Protoc 2: 891–903.
- 48, , , , ( 2007) Structural basis for the remarkable stability of Bacillus subtilis lipase (Lip A) at low pH. Biochim Biophys Acta 1784: 302–311.
- 49, , , , ( 2008) Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Arch Biochem Biophys 469: 20–28.
- 50, ( 1999) A thermodynamic comparison of mesophilic and thermophilic ribonucleases H. Biochemistry 38: 3831–3836.
- 51