Stability and stabilization of globular proteins in solution

Journal of Biotechnology

Volumn 79, Issue 3, 2000, Pages 193-203

  Jaenicke, Rainer ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Corresponding states; Extremophiles; Hyperthermophiles; Protein folding; Stabilization; Thermostability

Indexed keywords

AMINO ACID; CYSTINE; GLOBULAR PROTEIN; GLUTAMIC ACID; PROLINE; PROTEIN;

ADAPTATION; AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; CELL PH; CONFERENCE PAPER; ECOLOGY; ENERGY; ENTHALPY; ENTROPY; GENE SEQUENCE; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, FUNCTION AND VARIABILITY; SOLUTION AND SOLUBILITY; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

HYDROGEN BONDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEINS; SOLUTIONS; TEMPERATURE;

ACIDOPHILES;

EID: 0034717156     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(00)00236-4     Document Type: Conference Paper

References (75)

1. Adams, M.W.W., Kelly, R.M., 2000. Hyperthermophilic enzymes. Meth. Enzymol. (in press).
2. Auerbach G., Ostendorp R., Prade L. et al. LDH from the hyperthermophilic bacterium T. maritima: The crystal structure at 2.1 Å resolution reveals strategies for intrinsic stabilization. Structure. 6:1998;769-781.
3. Baldwin R.L. Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl. Acad. Sci. USA. 83:1986;8069-8072.
4. Barrett G.C. Chemistry and Biochemistry of Amino Acids. 1985;354-375 Chapman and Hall, New York.
5. Becktel W.J., Schellman J.A. Protein stability curves. Biopolymers. 26:1987;1859-1877.
6. Bernhardt G., Lüdemann H.-D., Jaenicke R., König H., Stetter K.O. Biomolecules are unstable under 'black smoker' conditions. Naturwissenschaften. 71:1984;583-586.
7. Bieri O., Kiefhaber T. Elementary steps in protein folding. Biol Chem. 380:1999;923-929.
8. Böhm G., Jaenicke R. On the relevance of sequence statistics for the properties of extremophilic proteins. Int. J. Pept. Protein Res. 43:1994;97-106.
9. Bryan P.N. Site-directed mutagenesis to study protein folding and stability. In: Protein Stability and Folding. Meth. Mol. Biol. 40:1995;271-289.
10. Carpenter J.F., Clegg J.S., Crowe J.H., Somero G.N. Compatible solutes and macromolecular stability. Cryobiology. 30:1993;201-241.
11. Chakrabartty A., Baldwin R.L. Stability of α-helices. Adv. Protein Chem. 46:1995;141-176.
12. Colacino F., Crichton R.R. Enzyme thermostabilization: the state of the art. Biotechnol. Genet. Eng. Rev. 14:1997;211-277.
13. Creighton T.E. On the relevance of non-random polypeptide conformations for protein folding. Biophys. Chem. 31:1988;155-162.
14. Deckert G., Warren P.V. et al., The complete genome sequence of the hyperthermophilic bacterium Aquifex aeolicus. Nature. 392:1996;353-358.
15. Dill K.A. Dominant forces in protein folding. Biochemistry. 29:1990;7133-7155.
16. Dill K.A., Privalov P.L., Gill S.J., Murphy K.P. The meaning of hydrophobicity. Science. 250:1990;297-298.
17. Eisenberg H. Life in unusual environments: progress in understanding the structure and function of enzymes from extreme halophilic bacteria. Arch. Biochem. Biophys. 318:1995;1-5.
18. Facchiano A.M., Colonna G., Ragone R. Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study. Protein Eng. 11:1998;753-760.
19. Franks F. Protein destabilization at low temperatures. Adv. Protein Chem. 46:1995;105-139.
20. Frolow F., Harel M., Sussman J.L., Mevarech M., Shoham M. Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin. Nat. Struct. Biol. 3:1996;452-458.
21. Groß M., Jaenicke R. Proteins under pressure: The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221:1994;617-630.
22. Hensel R., König H. Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol. Lett. 49:1988;75-79.
23. Huber R. Flexibility and rigidity of proteins and protein-pigment complexes. Angew. Chem. Int. Ed. 27:1988;79-99.
24. Ichikawa J.K., Clarke S. A highly active protein repair enzyme from the extreme thermophile T. maritima. Arch. Biophys. Biochem. 358:1998;222-231.
25. Jaenicke R. Folding and association of proteins. Progr. Biophys. Mol. Biol. 49:1987;117-237.
26. Jaenicke R. Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202:1991a;715-728.
27. Jaenicke R. Protein folding: local structures, domains, subunits and assemblies. Biochemistry. 30:1991b;3147-3161.
28. Jaenicke R. Protein folding and association: significance of in vitro studies for self-organization and targeting in the cell. Curr. Top. Cell. Reg. 34:1996a;209-314.
29. Jaenicke R. GAPDH from T. maritima: strategies of protein stabilization. FEMS Microbiol. Rev. 18:1996b;215-224.
30. Jaenicke R. What ultrastable proteins teach us about protein stabilization. Biochemistry (Moscow). 63:1998;312-321.
31. Jaenicke R. Folding and stability of domain proteins. Progr. Biophys. Mol. Biol. 71:1999;155-241.
32. Jaenicke R., Böhm G. Stabilization of proteins: what extremophiles teach us about protein stability. Curr. Opin. Struct. Biol. 8:1998;738-748.
33. Jaenicke, R., Böhm, G., 2000. Thermostability of proteins. Meth. Enzymol. (in press).
34. Jaenicke, R., Lilie, H., 2000. Folding and association of oligomeric and multimeric proteins. Adv Protein Chem (in press).
35. Jaenicke R., Schurig H., Beaucamp N., Ostendorp R. Structure and stability of 'hyperstable proteins': glycolytic enzymes from the hyperthermophilic bacterium T. maritima. Adv. Protein. Chem. 48:1996;181-269.
36. Kauzmann W. Some factors in the interpretation of protein denaturation. Adv. Protein. Chem. 14:1959;1-63.
37. Kern G., Schmidt M., Buchner J., Jaenicke R. Glycosylation inhibits the interaction of invertase with the chaperone GroEL. FEBS Lett. 305:1992a;203-205.
38. Kern G., Schülke N., Schmid F.X., Jaenicke R. Quaternary structure and stability of internal, external and core-glycosylated invertase from yeast. Protein Sci. 1:1992b;120-131.
39. Kern G., Kern D., Jaenicke R., Seckler R. Kinetics of folding and association of differently glycosylated variants of invertase from C. cerevisiae. Protein Sci. 2:1993;1862-1868.
40. Knapp S., Mattson P.T., Christova P. et al. Thermal unfolding of small proteins with SH3 domain folding. Proteins: Struct. Funct. Genet. 31:1998;309-319.
41. Korndörfer I., Steipe B., Huber R., Tomschy A., Jaenicke R. The crystal structure of holo-GAPDH from the hyperthermophilic bacterium T. maritima. J. Mol. Biol. 246:1995;512-521.
42. Lauffer M.A. Polymerization-depolymerization of TMVP. VII: a model. Biochemistry. 5:1966;2440-2446.
43. Lauffer M.A. Polymerization-depolymerization of TMVP: refinement of a model. Chimia. 21:1967;460-462.
44. Leibrock E., Bayer P., Lüdemann H.-D. Non-enzymatic hydrolysis of ATP at high temperatures and high pressure. Biophys. Chem. 54:1995;175-180.
45. Leikin S., Parsegian V.A. Temperature-induced complementarity as a mechanism for biomolecular assembly. Proteins. 19:1994;73-76.
46. Lifson S. Wanderings in the fields of science. Comprehensive Biochemistry. Semenza Ed. 40:1997;1-55.
47. Lifson S., Felder C.E., Libmann J., Shanzer A. The role of energy calculations in the design, synthesis and study of biologically active Fe(III) carriers. Wipff G. Computational Approaches to Supramolecular Chemistry. 1994;349-376 Kulver Acad. Publ, Dordrecht.
48. Makhatadse G.I., Privalov P.L. Energetics of protein structure. Adv Protein Chem. 47:1996;307-345.
49. Matthews B.W. Studies on protein stability with T4 lysozyme. Adv. Protein Chem. 46:1995;249-278.
50. Matthews B.W. Structural and genetic analysis of the folding and function of T4 lysozyme. FASEB J. 10:1996;35-41.
51. Minuth T., Frey G., Lindner P., Stetter K.O., Jaenicke R. Recombinant ultrastable chaperonin from the archaeon Pyrodictium occultum shows chaperone activity in vitro. Eur. J. Biochem. 258:1998;837-845.
52. Minuth T., Henn M., Rutkat K. et al. The recombinant thermosome from the hyperthermophilic archaeon Methanopyrus kandleri: in vitro analysis of its chaperone activity. Biol. Chem. 380:1999;55-62.
53. Murphy K.P. Non-covalent forces important to the conformational stability of protein structures. Shirley B.A. Protein Stability and Folding Meth. Mol. Biol. 40:1995;1-34.
54. Opitz U., Rudolph R., Jaenicke R., Ericsson L., Neurath H. Proteolytic dimers of LDH: characterization, folding and reconstitution or the truncated and nicked polypeptide chain. Biochemistry. 26:1987;1399-1406.
55. Pace C.N., Shirley B.A., McNutt M., Gajiwala K. Forces contributing to the conformational stability of proteins. FASEB J. 10:1996;75-83.
56. Pappenberger G., Schurig H., Jaenicke R. Disruption of an ionic network leads to accelerated thermal denaturation of GAPDH of the hyper-thermophilic bacterium T. maritima. J. Mol. Biol. 274:1997;676-683.
57. Peng Z.-Y., Wu L.C., Schulman B.A., Kim P.L. Does the molten globule have a native-like tertiary fold? Phil. Trans. R. Soc. Lond. B. Biol. Sci. 348:1995;43-47.
58. Perl D., Welker C., Schindler T. et al. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold-shock proteins. Nat. Struct. Biol. 5:1998;229-235.
59. Pfeil W. Protein Stability and Folding: A Collection of Thermodynamic Data. 1998;Springer, Berlin, Heidelberg, New York.
60. Privalov P.L. Stability of proteins. Adv. Protein Chem. 33:1979;167-241.
61. Privalov P.L., Gill S.J. The hydrophobic effect: a reappraisal. Pure Appl. Chem. 61:1989;1097-1104.
62. Ragone R. Protein association and stability of thermophilic enzymes. Protein Pept. Lett. 4:1997;277-279.
63. Ragone R., Colonna G. Do globular proteins require some structural peculiarity to best function at high temperatures? J. Am. Chem. Soc. 117:1995;16-20.
64. Rehaber V., Jaenicke R. Stability and reconstitution of GAPDH from the eubacterium T. maritima. J. Biol. Chem. 267:1992;10999-11006.
65. Schellman J.A. Temperature, stability and the hydrophobic interaction. Biophys. J. 73:1997;2960-2964.
66. Somero G.N. Environmental adaptation of protein: strategies for the conservation of critical functional and structural traits. Comp. Biochem. Physiol. A. 76:1983;621-633.
67. Somero G.N. Proteins and temperature. Annu. Rev. Physiol. 57:1995;43-68.
68. Trent J.D., Kagawa H.K., Yaoi T., Olle E., Zaluzec N.J. Chaperonin filaments: The archaeal cytoskeleton. Proc. Natl. Acad. Sci. USA. 94:1997;5383-5388.
69. Tsou C.-L. Folding of the nascent peptide chain into a biologically active protein. Biochemistry. 27:1988;1809-1812.
70. Tsou C.-L. The role of active site flexibility in enzyme catalysis. Biochemistry (Moscow). 63:1998;253-258.
71. Vita C., Fontana A., Jaenicke R. Folding of thermolysin fragments: hydrodynamic properties of isolated domains and subdomains. Eur. J. Biochem. 183:1989;513-518.
72. Volkin D.B., Mach H., Middaugh C.R. Degradative covalent reactions important to protein stability. In: Protein Stability and Folding. Meth. Mol. Biol. 40:1995;35-63.
73. Wallon G., Kryger G., Lovett S.T., Oshima T., Ringe D., Petsko G.A. Crystal structures of E. coli and S. typhimurium IPMDH and comparison with their thermophilic counterpart from T. thermophilus. J. Mol. Biol. 266:1997;1016-1031.
74. Wright P.E., Dyson H.-J., Lerner R.A. Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding. Biochemistry. 27:1988;7167-7175.
75. Závodszky P., Kardos J., Svingor A., Petsko G.A. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc. Natl. Acad. Sci. USA. 95:1998;7406-7411.