Stabilizing effect of polyols is sensitive to inherent stability of protein

Biophysical Chemistry

Volumn 156, Issue 1, 2011, Pages 68-71

  Kamal, Md Zahid ^a   Ahmad, Shoeb ^a   Rao, Nalam Madhusudhana ^a  

^a CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

Author keywords

Glycerol; In vitro evolution; Lipase; Polyol; Protein stability

Indexed keywords

GLYCEROL; MUTANT PROTEIN; TRIACYLGLYCEROL LIPASE;

ARTICLE; BODY SURFACE; CONTROLLED STUDY; ENZYME STABILITY; IN VITRO STUDY; MUTANT; PH; POLARIZATION; PRIORITY JOURNAL; PROTEIN INTERACTION;

BACILLUS SUBTILIS; GLYCEROL; LIPASE; MUTATION; PROTEIN DENATURATION; PROTEIN STABILITY;

EID: 79955967504     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2010.12.008     Document Type: Article

References (27)

1. P.R. vis-Searles, A.J. Saunders, D.A. Erie, D.J. Winzor, G.J. Pielak, Interpreting the effects of small uncharged solutes on protein-folding equilibria, Annu. Rev. Biophys. Biomol. Struct. 30 (2001) 271-306.
2. D. Knoll, J. Hermans, Polymer-protein interactions. Comparison of experiment and excluded volume theory, J. Biol. Chem. 258 (1983) 5710-5715.
3. O.G. Berg, The influence of macromolecular crowding on thermodynamic activity: solubility and dimerization constants for spherical and dumbbell-shaped molecules in a hard-sphere mixture, Biopolymers 30 (1990) 1027-1037.
4. P.R. Wills, Y. Georgalis, J. Dijk, D.J. Winzor, Measurement of thermodynamic nonideality arising from volume-exclusion interactions between proteins and polymers, Biophys. Chem. 57 (1995) 37-46.
5. A.P. Minton, Influence of excluded volume upon macromolecular structure and associations in 'crowded' media, Curr. Opin. Biotechnol. 8 (1997) 65-69.
6. C. Tanford, Extension of the theory of linked functions to incorporate the effects of protein hydration, J. Mol. Biol. 39 (1969) 539-544.
7. K. Gekko, S.N. Timasheff, Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures, Biochemistry 20 (1981) 4667-4676.
8. S.N. Timasheff, Solvent stabilization of protein structure, Meth. Mol. Biol. 40 (1995) 253-269.
9. S.N. Timasheff, Protein hydration, thermodynamic binding, and preferential hydration, Biochemistry 41 (2002) 13473-13482.
10. Y. Liu, D.W. Bolen, The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes, Biochemistry 34 (1995) 12884-12891.
11. J.K. Kaushik, R. Bhat, Thermal stability of proteins in aqueous polyol solutions: role of the surface tension of water in the stabilizing effect of polyols, J. Phys. Chem. B 102 (1998) 7058-7066.
12. M. Auton, A.C. Ferreon, D.W. Bolen, Metrics that differentiate the origins of osmolyte effects on protein stability: a test of the surface tension proposal, J. Mol. Biol. 361 (2006) 983-992.
13. A.J. Saunders, P.R. vis-Searles, D.L. Allen, G.J. Pielak, D.A. Erie, Osmolyte-induced changes in protein conformational equilibria, Biopolymers 53 (2000) 293-307.
14. I. Haque, R. Singh, A.A. Moosavi-Movahedi, F. Ahmad, Effect of polyol osmolytes on DeltaG(D), the Gibbs energy of stabilisation of proteins at different pH values, Biophys. Chem. 117 (2005) 1-12.
15. P. Acharya, E. Rajakumara, R. Sankaranarayanan, N.M. Rao, Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase, J. Mol. Biol. 341 (2004) 1271-1281.
16. S. Ahmad, M.Z. Kamal, R. Sankaranarayanan, N.M. Rao, Thermostable Bacillus subtilis lipases: in vitro evolution and structural insight, J. Mol. Biol. 381 (2008) 324-340.
17. O.V. Tsodikov, M.T. Record Jr., Y.V. Sergeev, Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature, J. Comput. Chem. 23 (2002) 600-609.
18. M.A.K. Markwell, S.M. Hass, N.E. Tolbert, L.L. Bieber, Protein determination in membrane and lipoprotein samples, Man. Automated Proced. (1981) 296-303.
19. J.C. Gordon, J.B. Myers, T. Folta, V. Shoja, L.S. Heath, A. Onufriev, H++: a server for estimating pK(a)s and adding missing hydrogens to macromolecules, Nucleic Acids Res. 33 (2005) W368-W371. (Pubitemid 44529945)
20. C. Tanford, Protein denaturation, Adv. Protein Chem. 23 (1968) 121-282.
21. E. Rajakumara, P. Acharya, S. Ahmad, V.M. Shanmugam, N.M. Rao, R. Sankaranarayanan, Crystallization and preliminary X-ray crystallographic investigations on several thermostable forms of a Bacillus subtilis lipase, Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 160-162. (Pubitemid 41295179)
22. E. Rajakumara, P. Acharya, S. Ahmad, R. Sankaranaryanan, N.M. Rao, Structural basis for the remarkable stability of Bacillus subtilis lipase (Lip A) at low pH, Biochim. Biophys. Acta 1784 (2008) 302-311.
23. J.K. Kaushik, R. Bhat, Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose, J. Biol. Chem. 278 (2003) 26458-26465.
24. I. Haque, A. Islam, R. Singh, A.A. Moosavi-Movahedi, F. Ahmad, Stability of proteins in the presence of polyols estimated from their guanidinium chloride-induced transition curves at different pH values and 25 degrees C, Biophys. Chem. 119 (2006) 224-233.
25. P. Cioni, E. Bramanti, G.B. Strambini, Effects of sucrose on the internal dynamics of azurin, Biophys. J. 88 (2005) 4213-4222. (Pubitemid 40991132)
26. A. Almagor, A. Priev, G. Barshtein, B. Gavish, S. Yedgar, Reduction of protein volume and compressibility by macromolecular cosolvents: dependence on the cosolvent molecular weight, Biochim. Biophys. Acta 1382 (1998) 151-156.
27. N. Taulier, T.V. Chalikian, Compressibility of protein transitions, Biochim. Biophys. Acta 1595 (2002) 48-70.