Temperature and pressure dependence of protein stability: The engineered fluorescein-binding lipocalin FluA shows an elliptic phase diagram

Proceedings of the National Academy of Sciences of the United States of America

Volumn 105, Issue 15, 2008, Pages 5756-5761

  Wiedersich, Johannes ^a   Köhler, Simone ^a   Skerra, Arne ^a   Friedrich, Josef ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Anticalin; Denaturation; Engineering; Folding; Thermodynamics

Indexed keywords

FLUORESCEIN BINDING LIPOCALIN FLUA PROTEIN; GLOBULAR PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; CORRELATION ANALYSIS; ENTHALPY; ENTROPY; EQUILIBRIUM CONSTANT; FLUORESCENCE; HEAT; MATHEMATICAL ANALYSIS; PRESSURE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE DEPENDENCE; THERMODYNAMICS; THERMOSTABILITY;

FLUORESCEIN; LIPOCALINS; PHASE TRANSITION; PRESSURE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; RECOMBINANT PROTEINS; TEMPERATURE; THERMODYNAMICS;

EID: 44449132615     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0710409105     Document Type: Article

References (43)

1. Brandts JF (1964) Thermodynamics of protein denaturation. I. Denaturation of chymotrypsinogen. J Am Chem Soc 86:4291-4301.
2. Brandts JF (1964) Thermodynamics of protein denaturation. 2. Model of reversible denaturation and interpretations regarding stability of chymotrypsinogen. J Am Chem Soc 86:4302-4314.
3. Hawley SA (1971) Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10:2436-2442.
4. Winter R, Dzwolak W (2005) Exploring the temperature-pressure configurational landscape of biomolecules: From lipid membranes to proteins. Philos Trans A Math Phys Eng Sci 363:537-562.
5. Silva JL, Foguel D, Royer CA (2001) Pressure provides new insights into protein folding, dynamics and structure. Trends Biochem Sci 26:612-618.
6. Hillson N, Onuchic JN, Garcia AE (1999) Pressure-induced protein-folding/unfolding kinetics. Proc Natl Acad Sci USA 96:14848-14853.
7. Onuchic JN, Wolynes PG (2004) Theory of protein folding. Curr Opin Struct Biol 14:70-75.
8. Dobson CM, Sali A, Karplus M (1998) Protein folding: A perspective from theory and experiment. Angew Chem Int Ed 37:868-893.
9. Hummer G, Garde S, Garcia AE, Paulaitis ME, Pratt LR (1998) The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc Natl Acad Sci USA 95:1552-1555.
10. Baldwin RL (1986) Temperature dependence of the hydrophobic interaction in protein folding. Proc Natl Acad Sci USA 83:8069-8072.
11. Baldwin RL, Muller N (1992) Relation between the convergence temperatures Th* and Ts* in protein unfolding. Proc Natl Acad Sci USA 15:7110-7113.
12. Privalov PL (1979) Stability of proteins: Small globular proteins. Adv Protein Chem 33:167-241.
13. Makhatadze GI, Privalov PL (1995) Energetics of protein structure. Adv Protein Chem 47:307-425.
14. Privalov PL, Gill SJ (1988) Stability of protein-structure and hydrophobic interaction. Adv Protein Chem 39:191-234.
15. Kauzmann W (1987) Protein stabilization - Thermodynamics of unfolding. Nature 325:763-764.
16. Hummer G, Garde S, Garcia AE, Paulaitis ME, Pratt LR (1998) Hydrophobic effects on a molecular scale. J Phys Chem B 102:10469-10482.
17. Panick G, et al. (1998) Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy. J Mol Biol 275:389-402.
18. Paschek D, Gnanakaran S, Garcia AE (2005) Simulations of the pressure and temperature unfolding of an -helical peptide. Proc Natl Acad Sci USA 102:6765-6770.
19. Paschek D, Garcia AE (2004) Reversible temperature and pressure denaturation of a protein fragment: A replica exchange molecular dynamics simulation study. Phys Rev Lett 93:238105.
20. Lesch H, Stadlbauer H, Friedrich J, Vanderkooi JM (2002) Stability diagram and unfolding of a modified cytochrome c: What happens in the transformation regime? Biophys J 82:1644-1653.
21. Doster W, Friedrich J (2005) Protein Folding Handbook, eds Buchner J, Kiefhaber T (Wiley-VCH, Weinheim, Germany), pp 99-126.
22. Heremans K, Smeller L (1998) Protein structure and dynamics at high pressure. Biochim Biophys Acta Protein Struct Mol Enzym 1386:353-370.
23. Zipp A, Kauzmann W (1973) Pressure denaturation of metmyoglobin. Biochemistry 12:4217-4228.
24. Smeller L, Heremans K (1997) High Pressure Research in the Biosciences and Biotechnology, ed Heremans K (Univ Press, Leuven, Belgium), pp 54-58.
25. Clark NA (1979) Thermodynamics of the re-entrant nematic-bilayer smectic A transition. J Phys Colloq C3 40:345-349.
26. Beste G, Schmidt FS, Stibora T, Skerra A (1999) Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. Proc Natl Acad Sci USA 96:1898-1903.
27. Skerra A (2000) Lipocalins as a scaffold. Biochim Biophys Acta Protein Struct Mol Enzym 1482:337-350.
28. Korndörfer IP, Beste G, Skerra A (2003) Crystallographic analysis of an "anticalin" with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region. Proteins 53:121-129.
29. Götz M, et al. (2002) Ultrafast electron transfer in the complex between fluorescein and a cognate engineered lipocalin protein, a so-called anticalin. Biochemistry 41:4156-4164.
30. Klug DD, Whalley E (1979) Relation between simple analytic models for optical-spectra of disordered solids. J Chem Phys 71:2903-2910.
31. Köhler M, Friedrich J, Fidy J (1998) Proteins in electric fields and pressure fields: Basic aspects. Biochim Biophys Acta Protein Struct Mol Enzym 1386:255-288.
32. Vopel S, Mühlbach H, Skerra A (2005) Rational engineering of a fluorescein-binding anticalin for improved ligand affinity. Biol Chem 386:1097-1104.
33. Lesch H, Hecht C, Friedrich J (2004) Protein phase diagrams: The physics behind their elliptic shape. J Chem Phys 121:12671-12675.
34. Frauenfelder H, Wolynes PG, Austin RH (1999) Biological physics. Rev Mod Phys 71:S419-S430.
35. Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG (1995) Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins 21:167-195.
36. Jäckle J (1983) The relation between the changes of thermodynamic quantities at the glass-transition and the long-wavelength fluctuations of glass structure. J Chem Phys 79:4463-4467.
37. Lubchenko V, Wolynes PG, Frauenfelder H (2005) Mosaic energy landscapes of liquids and the control of protein conformational dynamics by glass-forming solvents. J Phys Chem B 109:7488-7499.
38. Frank HS, Evans MW (1945) Free volume and entropy in condensed systems. 3. Entropy in binary liquid mixtures - Partial molal entropy in dilute solutions: structure and thermodynamics in aqueous electrolytes. J Chem Phys 13:507-532.
39. Briggs LJ (1950) Limiting negative pressure of water. J Appl Phys 21:721-722.
40. Dill KA (1985) Theory for the folding and stability of globular-proteins. Biochemistry 24:1501-1509.
41. Cheung JK, Shah P, Truskett TM (2006) Heteropolymer collapse theory for protein folding in the pressure-temperature plane. Biophys J 91:2427-2435.
42. Eremets MI (1996) High Pressure Experimental Methods (Oxford Univ Press, London).
43. Vos WL, Schouten JA (1991) On the temperature correction to the ruby pressure scale. J Appl Phys 69:6744-6746.