Enzyme thermostabilization: The State of the art

Biotechnology and Genetic Engineering Reviews

Volumn 14, Issue 1, 1997, Pages 211-278

  Colacino, Franco ^a   Crichton, Robert R ^a  

^a UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

STATE OF THE ART; THERMOSTABILIZATION;

ENZYME; PROTEIN;

CHEMICAL MODIFICATION; ENZYME STABILITY; GENETIC ENGINEERING; INDUSTRY; PROTEIN STABILITY; REVIEW; THERMOSTABILITY;

EID: 0031439744     PISSN: 02648725     EISSN: 20465556     Source Type: Journal    
DOI: 10.1080/02648725.1997.10647944     Document Type: Article

References (341)

1. CHEN, K, ROBINSON, A.C., VAN DAM, ME., MARTÍNEZ, P., ECONOMOU, C. and Arnold, F. (1991) Enzyme engineering for nonaqueous solvents, II, Additive effects of mutations on the stability and activity of subtilisin E in polar organic media, Biotechnology Progress, 7.125-129.
2. CHEN, J., Jo, S. and PARK, K. (1995), Polysacchnridc hydrogels for protein drug delivery, Carbohydrate Polymers. 28.69-76.
3. CHEN, B.L. and ARAKAWA, T. (1996), Stabilization of recombinant human keratinocyte growth factor by osmolytes and salts, Journal of Pharmaceutical Sciences, 85.419-422.
4. Chothia, C. (1974), Hydrophobic bonding and accessible surface area in proteins, Nature. 248, 338-339.
5. Cliothia C. (1984), Principles that determine the structure of proteins, Annual Review of Biochemistry, 83. 537-572.
6. CHOU, P, Y. and FASMAN, G.D. (1974), Conformational parameters for amino acids in helical, 3-sheet. and random coil regions calculated from proteins, Biochemistry. 13.213-245.
7. Cliou, P.Y. and FASMAN, G.D. (1978), Empirical predictions of protein conformation, Annual Review of Biochemistry. 47, 251-276.
8. Cion, F. (1995), Thermostabilization of erythrocyte carbonic anhydrase by polyhydric additives, Enzyme and Microbial Technology, 17.592-600.
9. Citri, N. (1973), Conformational adaptability in enzymes, Advances in Enzvmology, 37. 397-532.
10. Clarke, J. and Fersht, A. (1993), Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation, Biochemistry. 32.4322-4329.
11. CLELAND, J.C. and Langer, R.L. (1994), Formulation and delivery of proteins and peptides, ACS Symposium series. 567, 1-19.
12. COFFEY, J.W. and DE Duve, C. (1968), Digestive activity of lysosomes: I, the digestion of proteins by extracts of rat liver lysosomes, Journal of Biological Chemistry. 243, 3255-3263.
13. COHEN L.A. (1971) The Enzymes, Voi HI (Boyer, P.D., Ed), Academic Press, N.Y., 147-211.
14. COMBES, D., YOOVIDHYA, E., GIRBAL, E., WILLEMOT, R.M. and MONSAN, P. (1987), Effect of polyhydric alcohols on invertase stabilization. Annals of the N.Y. Academy of Science. 501. 69.
15. COOPER, A., EYLES, S.J., RADFORD, S.E. and DOBSON, CM. (1992), Thermodynamic consequences of the removal of a disulfide from hen lysozyme. Journal of Molecular Biology. 225, 939-943.
16. CORDES, M.H.J., DAVIDSON, A.R. and SAUER, R.T.S.O. (1996), Sequence space, folding and protein design. Current Opinion in Structural Biology, 6, 3-10.
17. CRABHE, M.J.C. (1990). In: Enzyme Biotechnology: protein engineering, Structure Prediction and Fermentation (Crabbe, M.J., Ed), Ellis Horwood, 11-60.
18. Craig, E.A., Weissman, J.S. and HORWICH, A.L. (1994), Heat-shock proteins and molecular chaperones: mediators of protein conformation and turnover in the ceil. Cell, 78, 365-372.
19. Creamer, T.P. and Rose, G.D. (1995), Interactions between hydrophobic side chains within alpha-helices. Protein Sc. 4, 1305-1314.
20. CREIGHTON, T.E. (1988), An empirical approach to protein conformation stability and flexibility. Biopolymers. 22.49-59.
21. Cunningham, B.C. and wells, J.A. (1987), Improvement in the alkaline stability of subtilisin using an efficient random mutagenesis and screening procedure. Protein Engineering, 1, 319-325.
22. Cupo P., EL-Deiry W., Whitney P. and Awad, W.M. (1980), Stabilization of proteins by guanidination. Journal of Biological Chemistry, 255(22), 10828-10833.
23. Cupo P., EL-DEIRY W., Whitney P. and Awad, W.M. (1982), Stability of acetylated and superguanidinatcd chymotry psinogen, Animal of Biochemistry and Biophisics.216,600-604.
24. DANIEL, R.M., COWAN, D.A., MORGAN, H.W. and CURRAN, M.P. (1982), A correlation between protein thermostability and resistance to proteolysis. Biochemical Journal. 207, 641-644.
25. DANIEL R.M., DINES, M. and PETACH, H.H. (1996), The dénaturation and degradation of stable enzymes at high temperatures. Biochemical Journal. 317, 1-11.
26. Dao-Pin, S., Sauer, U., Nicholson, H. and MATTHEWS, B.W. (1991), Contribution of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry. 3ft, 7142-7153.
27. DAY, M.W., and REES, D.C. (1992), X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic arehaebacterium. Pyrococcus furiasus, Protein Science, 1, 1494-1507.
28. Di-Cor T. S., Avila, I., HENDRICKX, M. and Tobback, P. (1994), DSC and protein-based time- tempcrattire integrators: case study of amylase stabilized by polyols and or sugar. Biotechnology and Bioengineering. 44, 859-8565.
29. DECLERCK, N., JOY ET, P., TROSSET, J.Y. and GARNIER, J. (1995), Hyperthermostable mutants of Bacillus licheniformis alpha amylase: multiple amino acid replacements and molecular modelling. Protein Engineering. 8, 1029-1037.
30. del Rio, G., Rodriguez, M.-E., Munguia, M.E., Lopez-Munguia, A. and Soberon, X. (1995), Mutant Escherichia coli penicillin acylase with enhanced stability at alkaline pH. Biotechnology and Bioengineering. 48, 141-148.
31. Delpino, I.M.P., SANCHEZERUIZ, J.M. (1995) An osmolyte effect on the heat capacity change for protein folding. Biochemistry. 34, 8621-8630.
32. DILL, K.A. (1985), Theory for the folding and stability of globular proteins. Biochemistry, 24. 1501-1509.
33. DILL, K.A. (1990), Dominant forces in protein folding. Biochemistry. 29, 7133-7155.
34. DOIG, A.J. and BALDWIN, R.L. (1995), N- and C-capping preferences for all 20 amino acids in alpha-helical peptides. Protein Science. 4, 1325-1336.
35. Doig, A.J. and WILLIAMS, D.H. (1991) Is the hydrophobic effect stabilizing or destabilizing in proteins ?The contribution of disulfide bonds to protein stability, Journal of Molecular Biology, 217, 389-398.
36. Dolla, A., Florens, L., Brusciii, M., Dudich, T.V. and Makarov, A.A. (1995), Drastic influence of a single heme axial ligand replacement on the thermostability of cytochrome c(3). Biochemical and Biophysical Research Communications. 211, 742-747.
37. Dordick, J.S. (1992) Design enzymes for use in organic solvents. Biotechnology Progress. 8, 259-267.
38. EIGHEN, M., GARDINER, W. (1984), Evolutionary molecular engineering based on RNA replication. Pure Appl, Chem., 56.967-978.
39. Eijsink, V.G.H., VRIEND, G., VAN DER ZEE, R., VAN DEN BURG, B. and VENEMA, G. (1992), Increasing the thermostability of the neutral proteinase Bacillus stearothermophilus by improvement of internal hydrogen-bonding. Biochemical Journal. 285.625-628.
40. Eijsink, v.g.H., Veltman, O.R., Aukema, W, Vriend, G. and Venema, G. (1995), Structural determinants of the stability of thermolysin-like proteinase. Nature Structural Biology. 2, 374-379.
41. Eriksson, A.E., Baase, w.a., Zhang, X.-JL, Heinz, D.W., Blaber, M., Baldwin, E.P., Matthews, B.W.(1992), Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science. 255, 178-183.
42. ERNST, J. A., CLUHB, R.T., ZHOU, H.-X., GRONEBORN, A. and CLORE, G.M. (1995), Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR. Science, 267. 1813-1817.
43. Estell, D. A., Graycer, T. P. and Wells, J.A.(1985), Engineering anenzymeby site-directed mutagenesis to be resistant to chemical oxidation. Journal of Biological Chemistry. 260, 6518-6521.
44. FAIRMAN, R., CHAO, H.-G., LAVOIE, T. B., VILLAFRANCA, J. J., MATSUEDA, G.R. and NOVTNY, J. (1996), Design of heterotetrameric coiled coils: evidence for increased stabilization by Glu-Lys+ pairs. Biochemistry, 35, 2824-2829.
45. feller, G., PAYAN, F., Theys, F., QIAN, M., HASER, R. and GERDA Y, C. (1994), Stability and structural analysis of α-amylase from the antartic psychrophile Alteromonas haloplanctis A23. European Journal of Biochemistry, 222, 441-447.
46. FERNANDEZLAFLUENTE, R., ROSELL, C.M., Alvaro, G. and GUISAN, J.M. (1992), Additional stabilization of penicillin G acylase-agarose derivatives by controled chemical modification with formaldehyde. Enzyme and Microbial Technology, 14,489-495.
47. FERNANDEZ-LAFLUENTE, R., ROSELL, C M., RODRIGUEZ, V. and GUISAN, J.M. (1995), Strategies for enzyme stabilization by intramolecular cross linking with bi functional reagents. Enzyme and Microbial Technology, 17, 517-523.
48. Ftorl, W.R., LUNDBERG, K.M. and Milhauser, G.L. (1994), A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptides. Nature Structural Biology. 1, 374-377.
49. Foster, T.M., Dormish, J.J., Narahari, U'Meyer, J.D., Vrklan, M., Henkin, J., Porter, W.R., Staack, H., Carpenter, J.F. and Manning, M.C. (1996), Thermal stability of low molecular weight urokinase during heat treatment, effect of salts, sugars. and Tween 80. International Journal of Pharmaceutics, 134, 193-201.
50. FRIEDMAN, F.K. and BEYCHOK, S. (1979), Probes of subunit assembly and reconstitution pathways in multi-subunit proteins. Annual Review of Biochemistry, 48, 217-250.
51. FROMMEL, C. and HOHNE, W.E. (1981), Influence of calcium binding on the thermal stability of thermitase, a serine protease from Themwactinomyces vulgaris, Biochemica and Biophysics Acta, 670, 25-33.
52. Fujii, M., Takage, M., Imanaka, T. and Aiba, S. (1983), Molecular cloning of a thermostable neutral protease gene from Bacillus stearothermophilus in a vector plasmid and its expression in Bacillus subtilis and Bacillus stearothermophilus, Journal of Bacteriology. 154. 831.
53. Galinski, E.A. (1993), Compatible solutes of halophilic eubacteria: molecular principles, water-solute interaction, stress protection. Experientia, 49, 487-496.
54. Gekas, V. and Lopez-Levia, M. (1985), Hydrolysis of lactose: a literature review. Process Biochew, 20, 2.
55. Gekko, K. and Timasheff, S.N. (1981), Thermodynamic and Kinetic examination of protein stabilization by glycerol. Biochemistry. 20, 4677-4686.
56. GEORGOPOULOS, C. and WELCH, W.J. (1993), Role of the major heat shock proteins as molecular chaperones. Annu, Rev, Cell, Biol., 9.601-634.
57. Gerbsch, N. and BUCHHOLZ, R. (1995), New processes and actual trends in biotechnology. FEMS Microbiology Reviews, 16, 259-269.
58. GERKEN, T.A., BUTENHOF, KJ. and SHOGREN, R. (1989), Effects of glycosylation on the conformation and dynamics of O-linked glycoprotein: C13 NMR studies of ovine submaxillary mucin. Biochemistty, 28, 5536-5543.
59. GERMAIN P., SLAGMOLEN T. and CRICHTON R.R. (1989), Relation between Stabilization and Rigidification of the Three-Dimensional Structure of an Enzyme. Biotechnology and Bioengineering, 33, 563-569.
60. Germain, P. and Crichton, R.R. (1988), Characterization of a chemically modified 13- amylase immobilized on porous silica. Journal of Chew, Tech, Biotechnol. 41.297-315.
61. GERMAIN, P., MAKAREN, J.S. and CRICHTON, R.R. (1988), Thermal stabilization of a chemically oriented modified pullulanase. Biotechnology and Bioengineering, 32.249-254.
62. Gmeiner, B., Leibl, H., Zerlauth, G. and SEELOS, C. (1995), Affinity binding of distinct functional fibronectin domains to immobilized metal chelates. Archives of Biochemistry and Biophysics, 32, 40-42.
63. Godavarti, R., Cooney, C.L., Langer, R. and Sisisekharan, R. (1996), Heparinase I from Flavobactcrium heparinum. identification of a critical histidine residue essential for catal y sis as probed by chemical modification and site-directed mutagenesis. Biochemistry. 35, 6846-6852.
64. Godfrey, T, and Reichelt, J. (1983), Industrial enzymology: the application of enzymes in industry, MacMillan Publisher Ltd.
65. Gokhale, R. S., Agarwalla, S., Santi, D.V. and Balaram, P. (1996), Covalent reinforcement of a fragile region in the dimeric enzyme thymidylate synthase stabilizes the protein against chaotrope-induced unfolding. Biochemistry. 35, 7150-7158.
66. Goodenough, P. W, and Jenkins, J. A. (1991), Protein engineering to change thermal stability for food enzymes. Biochemical Society Transaction, 19, 655-662.
67. Graciani, N.R., Tsang, K. Y., McCutchen, S. L. and Kelly, J.W. (1994), Amino acids that specify structure through hydrophobic clustering and histidine-aromatic interaction lead lo biologically active pepiidomimetics. Biorganic and Medical Chemistry, 2, 999-1006.
68. GRAY, C.J. (1988), Additives and enzyme stability. Biocatalysis. 1, 187-196.
69. Gray, C.J. (1993). In: Thermostability of Enzymes. (Gupta, M.N., Ed), Springer-Verlag Narosa Publishing House, 124-143.
70. Grimaldi, S., Giulani, A., Ferroni, L., Lisi, A., Santoro, N, and Pozzi, D. (1995), Engineered liposomes and virosomes for delivery of macromolecules. Research in Virology. 146, 289-293.
71. Gryk, M.R. and Jardetzky, O. (1996), AV77 hinge mutation stabilizes the helix-tum-helix domain of lip repressor. Journal of Molecular Biology. 255, 204-214.
72. Glisan, J.M., Alvaro, G., ROSELL, C. M, and FErnandez-Larjente, R. (1994), Industrial design of enzymic processes catalysed by very active immobilized derivatives: Utilization of diffusional limitations (gradients of pH), as a profitable tool in enzyme engineering. Biotechnology and Applied Biochemistly. 20(3), 357-369.
73. Gupta, M.N. (1991), Thermostabilization of proteins. Biotechnology and Applied Biochemistry. 14, 1-11.
74. GUPTA, M.N. (1992), Enzyme function in organic solvents. European Journal of Biochemistry. 203, 25-32.
75. Haltia, T and Freire, E. (1995), Forces and factors that contribute to the structural stability of membrane proteins. Biochemica and Biophysica Acta. 1228, 1-27.
76. Harris, J.L., Hocking, J.D., Runswick, M.J., Suzuki, K, and Walker, J.E. (1980), D- G3PDH, The purification and characterization of the enzyme from thermophiles is stearothemiophilus and Thenmisacfuaficus, European Journal of Biochemistry, 108, 535-542.
77. Harrison, P.M., and Sternberg, M.J.E. (1994), Analysis and classification of disufphide conneclivity in proteins: the enlropic effect of cross-linkage. Journal of Molecular Biology. 244.448-463.
78. Hartmeier, W. (1988). In: Immobilized Biocatalysts: an introduction, Springer-Verlag, 22-47.
79. Hayes, D.G, and Gulari, E. (1994), Improvement of enzyme activity and stability for reverse micellar-encapsulated lipases in the presence of short-chain and polar alcohols. Biocatahsis. 11, 223-238.
80. HEOHT, M.H., STURTEV ANTJ, and SAUER, R. (1984), Effect of single amino acid replacements on the thermal stability of the NH,-terminal domain of phage y repressor. Proceedings of the National Academy of Science USA. 81, 5685-5689.
81. Hendsch, Z.S, and Tidor, B. (1994), Do salt bridges stabilize proteins ? a continuum electrostatic analysis. Protein Science. 3, 211-226.
82. HOENES, J. (1985), Ligand binding and stabilization of Malale and Lactate dehydrogenase. Biol, Chem Hoppe-Seyler. 366, 561-566.
83. Hollecker, M, and Creighton, T. E. (1982), Effect on prolein stability of reversing the charge on amino groups. Biochintica and Biophysica Acta. 701, 395-4040.
84. Hora, J. (1973), Stabilization of Bacillus subtilis -amylase by amino group acylation. Biochimica and Biophysica Acta. 310, 264-267.
85. Horton, R.M., Hint, H.D, Ho, S.N., Pullen, J.K, and Pease, L.D. (1989), Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene. 77, 61-68.
86. HUSAIN, S., IQBAL, J, and SALEEMUDDIN, M. (1985), Entrapmentofconcanavalin A-glycoenzymc complexes in calcium alginate gels. Biotechnology and Bioengineering. 27, 1102.
87. HUSAIN, S., Jafki, F., SAIEKMUDDIN, M. (1996), Effects of chemical modification on the stability of invertasc before and after immobilization. Enzvme and Microbial Technology. 18, 275-280.
88. Huygiiues-Despointes, B. M. P., Klinger, T.M, and Baldwin, R.L. (1995), Measuringthe sirengh of side-chain hydrogen bonds in peptide helices: the Gln.Asp (i, i+4), interaction. Biochemistry, 34, 13267-13271.
89. ILLANES, A., ALTAIMIRANO, C, and ZUNIGA, M.E.(1996), Thermal inactivationof immobilized penicillin acylase in the presence of substrate and products. Biotechnology and Bioengineering. 30, 609-616.
90. IMANAKA, T., SHIBAZAKI, M, and TAKAGI, M. (1986), A new way of enhancing the thermostability of protease. Nature, 324, 695-697.
91. IMHOFF, J.F, and RODRIGUEZ-VALERA, F. (1986), Osmoregulation and compatible solutes in eubacteria. FEMS Microbiology Review. 139, 57-66.
92. IMPERIAL, B, and RICKERT, K.W. (1995), Conformational implications of asparagine-finked glycosylation. Proceedings of the National Academy of Science USA, 92, 97-101.
93. IWAKURA, M., JONES, B E, and MATTHEWS, C.R. (1995), A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli, Journal of Biochemistry. 117.480-488.
94. Jackson, S.E., Moracci, melMasry, N., Johnson, C.M, and Fersht, A. R. (1993), Effect of cavity creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry. 32, 11259-11269.
95. JAENTCKE, E. (1991) Protein folding: local structures, domains, subunits, assemblies. Biochemistry. 30, 3147-3161.
96. JANBON, G., DERANCOURT, J., CHEMARDIN, P., ARNAUD, A., GALZY P. (1995), A very stable beta-glucosidase from a Candida molischiana mutant strain: Enzymatic properties, sequencing. and homology with other yeast beta-ghicosidases. Bioscience Biotechnology and Biochemistry, 20, 1320-1322.
97. JIMENEZ, a., BRUIX, M., GONZALEZ, C., BLANCO, F.J., NIETO, J., HERRANTZ, J, and RICO, M. (1993), Studies on the conformational properties of peptide fragments from the C-terminal domain of thermolysin. European Journal of Biochemistry, 211, 569-581.
98. JOHNSON, R.E., ADAMS, P, and RUPLEY, J. A. (1978), Thermodynamics of protein cross-links. Biochemistry, 17, 1479-1484.
99. JOYET, P., DECLERK, N, and GAILLARDIN, C. (1992), Hyperthermostable variants of a highly thermostable alpha-amylase. Bio/Technology. 10, 1579-1583.
100. Ju, Y.H., CHEN, W.J, and LEE, C.K. (1995), Starch slurry hydrolysis using alpha-amylase immobilized on a hollow-fiber reactor. Enzyme and Microbial Technology, 17, 685-688.
101. KABSCH, W, and SANDER, C. (1983), Dictionary of protein secondary structure: pattern of recognition of hydrogen bonded and drug geometrical features. Biopolymers, 22, 2577-2637.
102. KAMBOJ, R.C., RAGHAV, N, and SINGH, H. (1996), Properties of cathepsin B immobilized in calciu m algi nate beads. Journal of Chemical Technology and Biotechnology. 65, 149-155.
103. KAMRA, A, and GUPTA, M.N.(1988a), Crosslinking of concavalin A with glutaraldehyde. Biochem, Int., 16, 679-687.
104. KAMRA, A, and GUPTA, M.N. (1988b), Reaction of concattavaltn A with dimethyl adipimidate: purification andcharacterizationofacrosslinkedconcanavalinAderivative with enhanced thermal stability. Biochemica and Biophvsica Acta, 966, 181-187.
105. Kato, Y., Aoki, T., Kato, N., Nakamura, R, and Matsuda, T. (1995), Modification of ovalbumin with glucose-6-phosphate by amino-carbonyl reaction, Improvement of protein heat stability and emulsifying activity. Journal of Agricultural and Food Chemistry. 43, 301-305.
106. KATZ, B.A, and KASSIAKOFF, A. (1986), The crystallographically determined structures of a typical strained disulfides engineered into substilisin. Journal of Biological Chemistry. 261, 15480-15485.
107. Kauzmann, W. (1959), Some factors in the interpretation of protein dénaturation. Advances in Protein Chemistry. 14, 1-63.
108. Kay, M.S, and Baldwin, R.L. (1996), Packing interactions in the apomyoglobin folding intermediate. Nature Structural Biology. 3, 439-145.
109. Kellis, J.T., NYBERG, K., SALI, D, and Fersht, A. (1988), Contribution of hydrophobic interactions to protein stability. Nature, 333, 784-786.
110. KEUL, V., KAEPPEU, F., GHOSH, C., KREBS, T., ROBINSON, J.A, and RETEY, J. (1979), Identification of the prosthetic group of urocanase, The mode of its reaction with sodium borohydride and of its photochemical reactivation. Journal of Biological Chemistry. 254, 8543-851.
111. Khan, S.M., Klibanov, A.M, Kaplan, N.O, and Kamen, M.D. (1981), The effect of electron carriers and other figands on oxygen stability of clostridial hydrogenase. Biochemica and Biophysica Acta. 659, 457-465.
112. Kher A. P. K, and Blumenth A. K. M.(1996), Importance of highly conserved anionic residues and electrostatic interactions in the activity and structure of the cardiotonic polypeptide anthopleurinB. Biochemistry, 35, 3503-3507.
113. Kim, C.W., Markifwicz, P.M., Lee, J.J., Schierle, C.F, and Miller, J.H. (1993), Studies of the hyperthermophile Thermotoga maritimaby random sequencing of cDNA and genomic libraries: identification an sequence of the tip EG(D). operon. Journal of Molecular Biology, 231.960-980.
114. KIRINO, h., AOKI, M., AOSHIMA, m., HAYASHI, Y., OHBA, M., YAMAGISHK A., WAKAGI, T, and OSHIMA, T. (1994), Hydrophobic interaction at the subunit interface contributes to the thermostability of 2-isopropy Inialate dehydrogenase from an extreme thcrmophilc,77fc?wiM.i thermophilus, European Journal of Biochemistry. 220, 275-281.
115. Kita, Y., Arakawa, T., Lin, T.-Y, and Timashepf, S.N. (1994), Contribution of the surface energy perturbation to protein-solvent interactions. Biochemistry. 33, 15178-15189.
116. KLEIJN, M, and NORDE, W. (1995), The adsorption of proteins from aqueous solution on solid surfaces. Heterogeneous Chemistry Reviews, 2, 157-172.
117. Klibanov, A.M. (1979a), Enzyme stabilization by immobilization. Analytical Chemistrv, 93, 1-25.
118. Klibanov, A.M. (1983), Immobilized enzymes and cells as practical catalysts. Science, 219, 722-727.
119. Klibanov, A.M., Kaplan, N.O, and Kamen, M.D. (1979), Chelating agents protect hydrogenase against oxygen inactivation. Biochemica and Bioplmica Acta. 547, 411-416.
120. Kolaskar, A.S, and Amelunxen, R.E. (1981), Conformation similarity among amino acid residues: 1, Analysis of protein crystal structure data. International J, Biol, Macromoi, 3, 171-178.
121. Kotik, M and Zuber H. (1993), Mutations that significantly change the stability, flexibility and quaternary structure of the l-LDH from Bacillus megaterium, European Journal of Biochemistry. 211, 267-280.
122. Kotsdka, T., Akanuma, S., Tomuro, M, and Yamagishi, T. (1996), Further stabilization of 3 isopropylmalate dehydrogenase of an extreme thermophile. Thermits thermophilus, by a suppressor mutation method. Journal of Bacteriology. 178, 723-727.
123. KREIAN, A., LORENZ, P., PLANA-COLL, M, and PYERIN, W. (1996), Interaction sites between catalytic and regulatory subunits in human protein kinaseCK2 holoenzymes as indicated by chemical cross-linking and immunological investigations. Biochemistry, 35, 4966-4975.
124. Kuhn, L., Swanson, D.A., Pique, M.E, and Tainer, J.A. (1995), Atomic and residue hydrophilicity in the context of folded protein structures. Proteins structure function and genetics. 23, 536-547.
125. KUHNVELTEN, W.N, and Lohr, J.B. (1996), Ligand dependence of cytochrome P450CI7 protection against proteolytic inactivation: structural, methodological and functional implications. FEBS Letters, 388, 21-25.
126. Kukarni, S.B., Betagerl G. V, and Singh, M. (1995), Factors affecting microencapsulation of drugs in liposomes. Journal of Microencapsulation, 12, 229-246.
127. Kumarasamy, R, and Symons, R.H. (1979), The tritium labeling of small amounts of protein for analysis by electrophoresis on sodium dodecyl sulfate-polyacrylamide slab gels. Analytical Biochemistiy, 95, 359-363.
128. Kupcu, S, Sara, M, and Sleytr, U.B. (1995), Liposomes coated with crystalline bacterial cell surface protein (S-layer) as immobilization structures for macromolecules. Biochemica and Biophysica Ada, 1235, 263-269.
129. Kwon, D. Y., Kim, P.S. (1994), The stabilizing effects of hydrophobic cores on peptide folding of bo vine-pancreatic-trypsin-inh i bi tor-intermediate mods. European Journal of Biochemistry. 223, 631-636.
130. Ladbury, J.E., Wynn, R., Thomson, J.A, and Sturtevant, J.M. (1995), Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heat capacity of the native protein. Biochemistry. 34, 2148-2152.
131. Le, W.P., Yan, S.X., Ll, S., Zhong, H.N., ZHOU, H.M. (1996), Alkaline unfolding and salt induced folding of yeast alcohol dehydrogenase under high pH conditions. International Jon mat of Peptide and Protein Research, 47, 484-490.
132. Lee, B. and Richards, P.M. (1976), The interpretation of protein structures: estimation of static accessibility. Journal of Molecular Biology. 55, 379-400.
133. Lee, J.C, and Timashefe, S.N. (1981), The stabilization of proteins by sucrose. Journal of Biological Chemistry, 256, 7193-7201.
134. Lenders, J.-P, and Crichton, R.R. (1984), Thermal stabilization of amylolytic enzymes by covalent coupling to soluble polysaccharides. Biotechnology and Bioengineering, 26, 1343-1351.
135. Lenders, J.-P., Germain, P, and Crichton, R.R. (1985), Immobilization of a soluble chemically thermostabilized enzyme. Biotechnology and Bioengineering, 27,572-578.
136. Lenders, J.-P, and Crichton, R.R. (1988), Chemical stabilization of glucoainylase from Aspergillus niger against thermal inactivation. Biotechnology and Bioengineering, 31, 267-277.
137. LEPOCK, J.R., FREY, H.E, and HALLEWELL, R.A. (1990), Contribution of conformational stability and reversibility of unfolding to the increased thermostability of human and bovine superoxide dismutase mutated at free cyst. Journal of Biological Chemistry. 265, 21612-21618.
138. Lethovaara, P.M., Koivula, A.K., Bameord, J, and Knowles, J.K.C. (1988), A new method for random mutagenesis of complete genes: enzymatic generation of mutant libraries in vitro, Protein Engineering, 2, 63-68.
139. LiCata, V.J, and Ackers, G.K. (1995), Long-range, small magnitude non-additivity of mutational effects in proteins. Biochemistry. 34, 3133-3139.
140. LINSKEO-CONNEL, L.I., Sherman, F, and McLendon, G. (1995), Stabilizing amino acid replacements at position 52 in Yeast iso-1-cytochrome c: in vivo and in vitro effects. Biochemistry. 34, 7094-7012.
141. Lio, H., Mckenzie, T, and Hageman, R. (1986), Isolation of a thermostable enzyme variant by cloning and selection in a thermophile. Proceedings of the National Academy of Science USA.83, 576-580.
142. LIS, H, and Sharon, N. (1993), Protein glycosylation: structural and functional aspects. European Journal of Biochemistry. 218, 1-27.
143. Liu W.R., Langer, R., and KUBANOV, A. M. (1991), Moisture Induced Aggregation of Lyophilized Proteins in the Solid State. Biotechnology and Bioengineering. 37, 177-184.
144. Livingstone, J.R., Spolar, R.S, and Thomas Record, M. (1991), Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. Biochemistry. 30, 4237-4244.
145. Lo, Y. Y, and Rahman, Y.E. (1995), Protein location in liposomes, a drug carrier: A prediction by differential scanning calorimetry. Journal of Pharmaceutical Sciences. 84.805-814.
146. Lopez-Camacho, C., Salgado, J., Lequerica, J.L., Madarro, A., Ballestar, E., Franco, L., and Plaina, J. (1996), Amino acid substitutions enhancing thermostability of Bacillus polymyxa 5-glucosidase. Biochemical Journal. 314, 833-838.
147. Lumry, R, and EYRING, H. (1954), Conformation changes of proteins. Journal of Physical Chemistry, 58, 110-120.
148. LUNDBLAD R.L, and NOYES C.M. (1985), Chemical reagents for protein modification, CRC Press, Boca Raton, Florida.
149. M aeda, Y., Yamada, H., Ueoa, T, and Imoto, T.(1996), Effectsof additives on the renaturation of reduced lysozyme in the presence of 4 M urea. Protein Engineering, 9,461-465.
150. Mainfroid, V., Mande, S.C., HOL, W.G.J., Martial, J. A, and GORAJ, K. (1996), Stabilization oflmman triosphosphate isomerase by improvement of the stability of individuala-helices in dimeric as well as monomeric forms of the protein. Biochemistry. 35,4110-4117.
151. Makino, Y., Negoro, S., Urabe, I, and Okada, H. (1989), Stability-increasing mutants of glucose dehydrogenase from Bacillus megaterium IWG3. Journal of Biological Chemis- try. 264, 6381-6385.
152. MANEEPUN, S, and KLIBANOV, A.M. (1982), Stabilization of microbial proteases against autolvsis using acylation with dicarboxylic acid anhydrides. Biotechnology and Bioengineering. 24.483-486.
153. MARAS b., CONSALVI v., CHIARALUCER., PoLm L., DEROSA M., BOSSA F., SCANDURRA R, and BARRA D. (1992), The protein sequence of glutamate dehydrogenase fromSulfolobus xolfatwicus a thermoacidopliilic archacbactcrium: is the presence of N-e-Methyllysine related to thermostability? European J, Biochemistry, 203, 81-87.
154. Markus, G. (1965), Protein substrate conformation and proteolysis. Proceedings of the National Academy of Science USA, 54, 253-258.
155. MARTINEK, K, and KLIBANOV, V.V. (1993). Thermostability of Enzymes (M.N.Gupia, Ed), Springer-Vcrlag Narosa Publishing House, 76-82.
156. Martino, A., Pifferi, P.G, and Spagna, G. (1996), Immobilization of 5-glucosida.se from a commercial preparation: optimization of the immobilization process on chitosan. Process Biochemistry. 31.287-293.
157. Matoba, S., Tsuneda, S., Saito, K, and Sugo, J. (1995), Highly efficient enzyme recovery using a porous membrane with immobilized tentacle polymer chains. Bio-Technoloev. 13, 795-797.
158. MATSI-KATA, M., Aoki, T., SANLI, K., OGATA, N, and KIKUC (1996), Effect of molecular architecture of poly(N-isopropylacrylamide), trypsin conjugates on their solution and enzymatic properties. Bioconjugate Chemistry. 7, 91-101.
159. MATSUMURA, M, and AIBA, S. (1985), Screening for thermostable mutant of kanamycin nucleotidyl transferase by the use of a transformation system for a thermophife. Bacillus .vtearothermophHus, J, Biol, Client., 260. 15298-15303.
160. MATSUMURA M., YASUMURA S, and Aiba S. (1986), Cumulative effect of intragenic amino-acid replacements on the thermostability of a protein. Nature. 323, 356-358.
161. MASTI-MTIRA, M., Becktel, W.J, and Matthews, B.W. (1988), Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of lie 3. Nature, 334, 406-410.
162. MATSUMURA M., BECKLTEL, W.J., LEVITT, M, and MATTHEWS, B.W. (1989a), Stabilization of phage T4 lysozyme by engineered disulfide bonds. Proceedings of the National Academy of Science USA. 86, 6562-6566.
163. MATSUMURA M., SIGNOR G, and Matthews B.W. (1989b), Substantial increase of protein stability by multiple disulphide bonds. Nature. 342, 291-293.
164. MATTHEWS, B.W. (1987a), Genetic and structural analysis of the protein stability problem. Biochemistry, 26.6885-6888.
165. MATTHEWS, B.W., NICHOLSON, H, and BECKTEL, W.J. (1987b), Enhanced protein thermostability from site-directed mutation that decreases the entropy of unfolding. Proceedings of the National Academy of Science USA. 84, 6663-6667.
166. Matthews, B.W. (1993), Structural and genetic analysis of protein stability. Annual Review of Biochemistry, 62, 139-160.
167. MATNIEWS, B.W. (1995), Can proteins be turned inside-out. Nature Structural Biology. 2, 85-86.
168. MOREE, D.E., REDFORD, S.M., GETZOFF, E.D., LEPOCK, J.R., HALLEWELL, R.A, and TAINER, J.A. (1990), Changes in crystallographic structure and thermostability of a Cu, Zn, superoxide dismutase mutant resulting from the removal of a buried cysteine. Journal of Biological Chemistry, 265. 14234-14241.
169. MEANS G.E, and Feeney R.E. (1971), Chemical Modification of Proteins, Holden-Day Inc., San Francisco, USA.
170. MEEKER, A.K., GARCIA-MORENO, B, and SHORTLE, D. (1996), Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. Biochemistiy, 35, 6443-6449.
171. MELIK-NUBAROV, N.S., MOZHAEV, V.V., SIKSNIS, S, and MARTINEK, K. (1987), Protein stabilization viahydrophilization: stabilization ofa-chymotrypsin by reductive alkylation with glyoxylic acid. Biotechnol letters. 10, 725.
172. MENENDE-ZARIAS, L, and ARGOS, P. (1989), Engineering protein thermal stability, Sequence sta-tistic point to residue substitutions ina-helix. Journal of Molecular Biology, 206, 397-406.
173. Mer, G., Hietter, H, and Lefevre, J.-L. (1996), Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor. Nature Structural Biology. 3.45-53.
174. MERKLER, D.J., FARRINGTON, G.K, and WEDLER, F.C. (1981), Protein thermostability. International Journal of Peptide and Protein Research. 18,430-442.
175. MERUTKA, G, and STELLWAGEN, E. (1990), Positional independence and additivity of amino acid replacements on hefix stability in monomeric peptides. Biochemistry. 29, 894-898.
176. Michels, A. A., Nguyen, V. T., Konings, A. W T., Kampinga, H. H, and Bensaudf, O. (1995), Thermostability of a nuclear-targeted luciferase expressed in mammalian cells: destabilizing influence of the intranuclear microenvironment. European Journal of Biochemistry, 234, 382-389.
177. Milla, M.E., Brown, B.B, and SAUER, R.T. (1994), Protein stability effects of a complete set of alanine substitutions in Arc repressor. Nature Structural Biology, 1, 518-523.
178. Minor, D.L., KIM, P.S.S.O. (1996), Context dependent secondary structure formation of a designed protein sequence. Nature, 380, 730-734.
179. Minotani, N., Sekeguchi, T., Bautista, J.G, and Nosoh, Y.(1979), Basis of thermostability in pig heart lactate dehydrogenase treated withi/-methylisourea. BiochemicaaitdBiophvsica Acta. 581, 334-341.
180. Mollah, A.K.M.M., Aleman, M.A., Albright, R.A, and Mossing, M.C. (1996), Core packing defects in an engineered Cro monomer corrected by combinatorial mutagenesis. Biochemistry, 35, 743-748.
181. MONSAN, P, and COMES, D. (1984), Mechanism of enzyme stabilization. Annals of the N.Y, Academy of Science. 434, 61-63.
182. MONTERNO, C., LLORENTE, p., ARGOMANÏZ, L, and MENENDEZ, M. (1996), Thermal stability of artemia HGPRT: effect of substrates on inactivation kinetics. International Journal of Biological Macromolecules, 18, 255-262.
183. MORENO, J. M, and OFAGAIN, C. (1996), Stabilization of alanine aminotransferase by consecutive modification and immobilization. Biotechnology Letters, 18, 51-56.
184. MOZHAEV V.V, and MARTINEK, K. (1984), Structure-stability relationships in proteins: new approaches to stabilizing enzymes. Enzyme Microbial technology, 6, 50-59.
185. Mozhaev v.v., siksnis v.a., Melik-Nubarov N.S., Galkantaite N.Z., Denis G.J., Butkus E.P., Zaslavsky B.Y., Mestechkina N.M, and Martinek, K. (1988), Protein stabilization via hydrophilization: covalent modification of trypsin and a-chymotrypsin European Journal of Biochemistry, 173, 147.
186. Mozhaev, V.V, and Melik-Nubarov, N.S. (1990), Strategy for stabilizing enzymes II: increasing enzyme stability by selective chemical modification. Biocatalysis, 3,189-186.
187. MRABET, N.T., SHAEFFER, J.R., MACDONALD, M.J, and BUNN, H.F. (1986), Dissociation of dimers of human hemoglobins A and F into monomers. Journal of Biological Chemistry. 261, 1111-1115.
188. Mrabet N.T., Van den Broeck A., Van den brande I., Stanssens P., Laroche Y., Lambeir A.-M., Matthijssens G., Jenkins, J, Chiadmi, M, van Tilbeurgh, H, Rey, F., Janinjquax, W.J., Lasters, I., De Mayer, M, and Wodak Shoshana (1993), Arginine residues as stabilizing elements in proteins. Biochemistry, 31,2239-2253.
189. Muller J. (1981), Stability of lactate dehydrogenase: chemical modification of lysines. Biochimica and Biophysica Acta, 681, 210-215.
190. Munôz, V, and SERRANO, L. (1994a), Elucidating the folding problem of helical peptides using empirical parameters. Nature Structural Biology, 1, 399-409.
191. Munôz, V, and SERRANO, L. (1994b), Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales. Proteins, 20, 301-311.
192. Munôz, V, and SERRANO, L. (1995), Elucidating the folding problem of helical peptides using emperical parameters, II Helix macrodipole effects and rational modification of the helical content of natural peptides. Journal of Molecular Biology, 245, 275-296.
193. Munôz, V., Blanco, F. J, and Serrano, L. (1995), The hydrophobic-staple motif and a role for loop-residues in a-helix stability and protein folding. Nature Structural Biology, 2. 380-385.
194. MURTHY, B.S., DELORENZO, CPICCOLI, R., DALESSJO, G, and SIRDESHMUKH, R. (1996), Effects of protein RNase inhibitor and substrate on the quaternary structures of bovine seminal RNase. Biochemistry, 35, 3880-3885.
195. NATH, D, and RAO, M. (1995), Increase in stability of xylanase from an aikalophilic thermophilic Bacillus (NCIM59), Biotechnology Letters, 17.557-560.
196. NEWSTED, W J, RAMJEESINGH, M, ZYWULKO, MLROTHSTEIN, S.J, and SHAMI, E.Y. (1995), Engineering resistance to trypsin inactivation into L-asparaginase through the production of a chimeric protein between the enzyme and a protective single-chain antibody. Enzyme and Microbial Technology. 17, 757-764.
197. Nicholls, D.J., Wood, S, Nobbs, T, Clarke, A.R., Holbrook, J.J., Atkinson, T, and Scawen, M.D. (1993), Dissecting the contributions of a specific side-chain interaction to folding and catalysis of Bacillus stearothermophHlus lactate dehydrogenase. European Journal of Biochemistry. 212,447-455.
198. Nicholson H., Becktel W.J, and Matthews B, W. (1988), Enhanced protein thermostability from designed mutations that interact with x helix dipoles. Nature, 336,651-656.
199. NICHOLSON, H, and ERSON, D.E., DAO-PIN, S., and Matthews, B.W. (1991), Analysis of the interaction between charged side chains and the oc-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry. 30, 9816-9828.
200. NIRASAWA, S., NISHINO, T., KATAHIRA, M., UESUGJ, S., HU, Z., and KURIHARA, Y. (1994), Structure of heat-stable and unstable homologues of the sweet protein: the difference in the heat stability is due to replacement of a single amino acid residue. European Journal of Biochemistiy. 223, 989-995.
201. NOLAN, R.D, and DAVIES, A. (1990), Fermentation biotechnology. hi: Enzyme Biotechnology: protein engineering, structure prediction and fermentation (Crabbe, M.J.C., Ed), Ellis Horwood, 97-125.
202. NOSOH, Y, and Sekiguchi, T. (1990), Protein engineering for thermostability. Trends in Biotechnology. 8, 16-20.
203. Nozaki, Y; and TANFORD, C. (1971), The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Journal of Biological Chemistrv, 246, 2211-2217.
204. O’FAGAIN, C, OKENNEDY, R, and KILTY, C. (1991), Stability of alanine aminotransferase is enhanced by chemical modification. Enzyme Microb, Technology, 13,234-239.
205. O’Fagain, C., Sheehan, H., O’Kennedy, R, and Kilty, C. (1988), Maintenance of enzyme structure: possible methods for enhancing s I abi I i ty. Process Biochemistry, Dec 1988, 166-171.
206. O’Neil, K.T, and DEGRADO, W.F. (1990), A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids. Science, 250,646-650.
207. Oakes, J. (1976), Thermally denatured proteins. Journal of the Chemical society faraday transactions. 72.228-237.
208. OLIVEBERG, M, and FERSHT, A.R. (1996a), Formation of electrostatic interactions on the protein-folding pathway. Biochemistry, 35, 2726-2737.
209. Oliveberg, M, and Fersht, A.R. (1996b), A new approach to the study of transient protein conformations: the formation of a semiburied salt link in the folding pathway of bamase. Biochemistry. 35, 6795-6805.
210. OLPHANT, A.R, and STRUHL, K. (1989), An efficient method for generating proteins with altered enzymatic properties: application to p-lactamaxe. Proceedings of the National Academy of Science USA, 86.9094-9098.
211. OSHIMA, T., NISHIDA, N., BAKTHAVATSALAM, S., KATAOKA, K., TAKADA, H, YOSHIMURA, T., ESAKI, P., NANDSODA, K. (1994), The purification, characterization, cloning and sequencing of the gene for a halostable and thermostable leucine dehydrogenase from Thermoactinomyces intermedins, European Journal of Biochemistry, 222, 305-312.
212. OSHIMA, T. (1994), Stabilization of proteins by evolutionary molecular engineering techniques. Current Opinion in Structural Biology, 4, 623-628.
213. OTZEN, D.E, and FERSHT, A.R. (1995), Side-chain determinants of P-sheet stability. Biochemistiy. 34, 5718-5724 (1995).
214. PACE, C.N, and MCGRATH, T. (1980), Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation. Journal of Biological Chemistry, 255, 3862-3865.
215. PACE, C.N., GRIMSLEY, G.R., THOMSON, J.A, and BARNET, B.J. (1988), Conformational stability and activity of ribonucleaseTI with zero, one, two intact disulfide bonds. Journal of Biological Chemistry, 263, 11820-11825.
216. PACE, C.N. (1990a), Conformational stability of globular proteins. Trends in Biochemical Sciences, 15, 14-17.
217. Pace, C.N., LAURENTS, D.V, and THORNTON, J.A. (1990), pH dependence of the urea and guanidine hydrochloride dénaturation of ribonuclease A and ribonuclease TI. Biochemistry, 29, 2564-2572.
218. Pace, C.N. (1990b), Measuring and increasing protein stability. Trends in Biotechnology. 8, 93.
219. PACE, C.N., Shirley, B.A., McNurr, M, and GAJIWALA, K. (1996), Forces contributing to the conformational stability of proteins. FASEB Journal. 10, 75-83.
220. PACE, N. (1992), Contribution of the hydrophobic effect to globular protein stability. Journal of Molecular Biology. 222, 29-35.
221. PADM ANABHAN, S., York, E.J., Stewart, J.M, and Baldwin, R.L. (1996), Helix propensities of basic amino acids increase with the length of the side chain. Journal of Molecular Biology. 257.726-734.
222. PAKULA, A.A, and Sauer, R.T. (1990), Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface. Nature. 344.363-364.
223. PANTOLIANO, M.W., WHITLOW, M., WOOD, J.F., DODD, S.W, HARDMAN, K.D., ROLLENCE, M.L, and BRYAN, P. (1989), Large Increases in General Stability for Subtilisin BPN through Incremental Changes in the Free Energy of Unfolding. Biochemistry, 28, 7205-7213.
224. Pantoliano, M.w, Ladner, R.C., Bryan, P.N., Rollence, M.L., Wood, J.F, and Poulos, T. (1987), Protein engineering of subtilisin BPN': enhanced stabilisation through the introduction of two cysteines to form a disulfide bond. Biochemistry, 26, 2077-2082.
225. PANTOLIANO, M.w., WHITLOW, m., WOOD, J.F., ROLLENCE, M.L., FINZEL, B.C., GILLILAND, G.L., POULOS, T.L, and BRYAN, P. (1988), The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case. Biochemistry. 27, 8311-8317.
226. Parsell, D. A, and Lindquist, S. (1993), The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annual Revue of Genetic. 27, 437-496.
227. PAUIING, L, and Corey, R.B. (1951), Configurations of polypeptide chains with favored orientations around single bonds: two new pleated sheets. Proceedings of the National Academy of Science USA. 37, 729-740.
228. Pauling, L, and Corey, R.B, and Branson, H.R. (1951), The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain. Proceedings of the National Academy of Science USA. 37,205-211.
229. PEITSCII, M.C. (1996), ProMod and Swiss-Model: internet-based tools for automated comparative protein modelling. Biochemical Society Transactions. 24, 275-279.
230. PEREZ-PAYA, E., HOUGHTEN, R.A, and BLONDELLE, S.E. (1996), Functionalized protein-like structures from conformationally defined synthetic combinatorial libraries. Journal of Biological Chemistry, 271, 4210-4126.
231. PETUKHOV, M., YUMOTO, N., MURASE, S., ONMURA, R, and YOSHIKAWA, S. (1996), Factors that affect the stabilization of a-helices in short peptides by a capping box. Biochemistry. 35, 387-397.
232. PICKERSGILL, R.W., SUMNER, I.G., COLLINS, M.E., WARWICKER, J., PERRY, B., BHAT, M.K, and GOOGENOUGH, P.W. (1991) Modification of the stability of phosphoiipase A2 by charge engineering. FEBS Letters. 281, 219-222.
233. Pielak, G.J., Auld, D.S., Beasley, J.R., Betz, S.F., Cohen, D.S., Doyle, D.F., Finger, S.A., Fredericks, L., Hilgen-Willis, S, Saunders, A.J, and Trojak, S.K. (1995), Protein thermal dénaturation, side-chain models. and evolution: amino acid substitutions at a conserved helix-helix interface. Biochemistry. 34, 3268-3276.
234. PILLER, K., DANIEL, P.M, and PETACH, H.H. (1996), Properties and stabilization of an extracellular glucosidase from the extremely thermophilic archaebacteria Thermococcus strain AN I: enzyme activity at 130°C. Biochemica and Biophysica Acta, 129, 197-205.
235. POHL, M., MESCH, K., RODENBROCK, A, and KULA, M R. (1995), Stability investigations on the pyruvate decarboxylase from Zymomonas mobilis, Biotechnology and Applied Biochemistry, 22, 95-105.
236. Ponder, J.W, and Richards, P.M. (1987), Tertiary templates for proteins: use of packing criteria in the enumeration of allowed sequences for different structural classes. Journal of Molecular Biology, 193,775-791.
237. PONNUSWAMY, P.K., PRABHAKARAN, M, and MANAVALAN, P. (1980), Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins. Biochemica and Biophysica Acta. 623, 301-316.
238. Pontius, B.W. (1993), Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association. Trends in Biochemical Sciences, 18, 181-186.
239. POWELL, L.M., PAIN, R.H. (1992), Effect of glycosylation on the folding and stability of human, recombinant and cleaved a-antitrypsin. Journal of Molecular Biology, 224, 241-252.
240. Predky, P.F., Agrawal, V., Brunger, A.T, and Regan, L.(1996), Amino acid substitutions in a surface turn modulate protein stability. Nature Structural Biology, 3, 54-58.
241. PRIEV, A., ALMAGOR, A., Yedgar, S, and Gavish, B. (1996), Glycerol decreases the volume and compressibility of protein interior. Biochemistry, 35.2061-2066.
242. PURL M., MARWAHA, S.S, and KOTHARI, R.M. (1996), Studies on the applicability of alginate entrapped naringinase for the debittering of kinnow juice. Enzyme and Microbial Technology. 18, 281-285.
243. QIAN, H. (1996), Prediction of helices in proteins based on thermodynamic parameters from solution chemistry. Journal of Molecular Biology, 256, 663-666.
244. QUAW, F.S, and BREWER, J.M. (1986), Arginyl residues and thermal stability in proteins. Mol, Cell, Biochem. 71, 121-127.
245. RADZICKA, A, and WOLFENDEN, R. (1988), Comparing the polarities of the amino acids: side- chain distribution coefficients between the vapor phase, cyclohexane, l-octanol. and neutral aqueous solution. Biochemistry, 27, 1644-1670.
246. RAIRY, R.V., BEC, N., SALDANA, J.L., NAMETKIN, S.N., MOZHAEV, V.V., KLYACHKO, N.L., Levashov, A.V., BALNY, C. (1995), High-pressure stabilization of alpha-chymotrypsin entrapped in reversed micelles of Aerosol OT in octane against thermal inactivation. FEBS Letters, 364, 98-100.
247. REES, D.C, and ADAMS, M.W.W. (1995), Hyperthermophiles: taking the heat and loving it. Structure. 3, 251-254.
248. REETZ, M.T., ZONTA, A, and SIMPELKAMP, J. (1996), Efficient immobilization of lipase by entrapment in hydrophobic sol gel materials. Biotechnology and Bioengineering, 49, 527-534.
249. REITER, Y., ULRICH, B., KREJTMAN, R.J., JUNG, S.H., LEE, B, and PASTAN, I. (1994), Stabilization of the Fv fragments in recombinant immunotoxins by disulfide bonds engineered into conserved framework regions. Biochemistry, 33,5451-5459.
250. RICHARDSON, J.S, and RICHARDSON, D.C. (1988), Amino acid preferences for specific locations at the end of or-hcliccs. Science, 240, 1648-1652.
251. ROBERTSON, D, NOLL, D., ROBERTS, M.F., MENAIA, J, and BOONE, R.D. (1990), Detection of the osmoregulator betaine in methanogens. Applied Environmental Microbiology, 56, 563-565.
252. Roig, M.G., KENNEDY, J.F. (1995), Perspectives of biophysicochemical modifications of enzymes. Journal of Biomaterial Science-Polymer edn, 7, 1-22.
253. Ron, E., Freeman, A, and Solomon, B. (1995), Stabilization and surface modification of monoclonal antibodies by 'bi-layer mcagement'. JournalofhmnunolagicalMethods, 180, 237-245.
254. ROSELL, C.M., FBRNANDEZ-LAFLUENTE, R, and GUISAN, J.M. (1995), Modification of enzyme properties by the use of inhibitors during their stabilisation by multipoint covalent attachment. Biocatalysis and Biotransformation. 12, 67-76.
255. RUDD, P.M., Joao, H.C., Coghill, E., Fiten, P., Sanders, M R., Opdenakker, G, and Dwek, R.A. (1994), Glycoforms modify the dynamic stability and functional activity of an enzyme. liiocheimstiy. 33, 17-22.
256. ROECC, C., Ammer, D, and Lerch, K. (1982), Comparison of amino acid sequence and thermostalility of tyrosinase from three wild type strains of Neurospora crassa, Journal of Biological Chemistry. 257, 6420-6426.
257. Sali, D., Bycroit, M, and Fersht, A.R. (1988), Stabilization of protein structure by interaction of ot-helix dipole with a charged side chain residue. Nature. 335.740-745.
258. Sali, D., BYCROPT, M, and FIRSHT, A.R. (1991) Surface electrostatic interactions contribute little to stability of barnase. Journal of Molecular Biology. 220, 779-788.
259. SANCHO, J, SERRANO, L, and FERSHT, A.R. (1993), Histidine residues at the N- and C-termini of "-helices: perturbed pKas and protein stability. Biochemistry. 31, 2253-2258.
260. SANDBERG, W.S., TERWILLIGER, T.C. (1991), Energetics of repacking a protein interior. Proceedings of the National Academy of Science USA, 88, 1706-1710.
261. Santoro, M.M., Liu, Y., Khan, S.M.A., Hou, L-X and Bolen, D.W. (1992), Increased thermal stability of proteins in the presence of naturally occurine osmolites. Biochemistry, 31.5278-5283.
262. SARENCVAT, FIRHONEN, J., CANTELLL, K., and JULKUNEN, I. (1995), N-glycosylation of human interferon-y: glycans at Asn-25 are critical for protease resistance. Biochemical J., 308, 9-14.
263. SCHBLMAN, J.A. (1955), The thermodynamics of urea solutions and the heat of formation of the peptide hydrogen bond. Compt, Rend, lab, Carlsberg, Ser, Chim. 29, 228-260.
264. SCWNOMIYA, S., YAMANE, K, and OSHIMA, T. (1980), Isolation of a Bacillus subtilis transformant producing thermostablea-amylase by DNA from a thermophilic bacterium. Biochemical Biophysical Research Communication, 96, 175-179.
265. Schmidt R.D. (1979), 'Stabilized soluble enzymes' In: Advances in Biochemical Engineering (Ghose, T.K., Fiechter, A. and Blackebrough, eds), Vol 12.41-117.
266. SCHREIBER, G, and FERSHT, A.R. (1996), Rapid, electrostatically assisted association of proteins. Nature Structural Biology. 3, 427-431.
267. SCHUMMER, M. (1991), Stabilités et activités de iysozytnes spécifiquement monoacétylés, Thèse de doctorat UCL.
268. SERINA, L., BUCURENCI, N., GILLES, A.M., SUREWICZ, W.K., FABIAN, H., MANTSCH, H.H., TAKAHASHI, M., PETRESCU, I., BATELIER, G, and ARZU, O. (1996), Structural properties of UMP kinase from Escherichia Coii: modulation of protein solubility by pH and UTP. Biochemistry. 35, 7003-7011.
269. SERRANO, L, and FERSHT, A.R. (1989), Capping and a-helix. Nature. 342, 296-299.
270. Serrano, L., Horovitz, A, Avron, B., Bycroft, M, and Fersht, A.R. (1990), Estimating the contribution of engineered surfaceelectrostatic interactions to protein stability by using double mutant cycles. Biochemistry, 29, 9343-9352.
271. Serrano, L., Kellis, J.T., Cann, P., Matouschek, A., and Fersht, A. (1992), The folding of an enzyme: li, Substructure of barnase and the contribution of different interactions to protein stability. Journal of Molecular Biology, 224, 783-804.
272. SERRANO, L., Neira, J.-L., Sancho, J, and Fersht, A.R. (1993), A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. Journal of Molecular Biology, 233, 205-312.
273. SHAH, B, Kumar S.R, & Devi, S. (1995), Immobilized proteolytic enzymes on resinous materials and their use in milk-clotting. Process Biochemistry, 30, 63-68.
274. SHAKED, Z, and WOLFE, S. (1988), Stabilization of pyranose 2-oxidase and catalase by chemical modification. Methods in Enzynwlogy. 137, 599-615.
275. Shami, E., ROTHSTEIN, A, and Ramjeesingh, M. (1989), Stabilization of biologically active proteins. Trends in Biotechnology, 7, 186-190.
276. Siiatsky, M. A., Ho, H.C, and Wang, J.H.-C.(1973), Stabilization of glycogen phosphoryiase b by reductive alkylation with aliphatic aldehydes. Biochirnica andBiophvsica Acta, 303, 298-307.
277. SHIBUYA, H, ABEMLSEKIGUCHI, T, and NOSOH, Y. (1982), Effect of guanidmation on subunit i nterac t ions in hybrid isozymes from pig lac tate dehydrogenase. Biochirnica and Biophvsica Ada. 708, 300-304.
278. SHIRLEY, B.A., STANSSENS, P, HAHN, U, and PACE, C.N. (1992), Contribution of hydrogen bonding to the conformational stability of ribonuclease T,. Biochemistry, 31, 725-732.
279. SHOICHET, B.K., BAASE, W.A., Kuroki, R, and MATTHEWS, B.W. (1995), A relationship between stability and protein function. Proceedings of the National Academy of Science USA. 92, 452-456.
280. Shun-Cheng, L, and Deber, C M. (1994), A measure of helical propensity for amino acids in membrane environments. Nature Structural Biology, 1, 368-373.
281. Sneddon, S.F, and Tobias, D.J. (1992), The role of packing interactions in stabilizing folded proteins. Biochemistiy. 31, 2842-2846.
282. Spolar, R.S., Ha, J.-H, and Record, M.T. (1989), Hydrophobic effect in protein folding and other noncovalent processes involving proteins. Proceedings of the National Academy of Science USA. 86, 8382-8385.
283. STITES, W.E, and Pranata, J. (1995), Empirical evaluation of the influence of side chains on the conformational entropy of the polypeptide backbone. Protein: Structure Function and Genetics, 22. 132-140.
284. STRUII LOW, K.G, and Baldwin, R.L. (1989), Effect of the substitution AlaGly at each of five residue positions in the C-peptide helix. Biochemistiy. 1989, 2130-2133.
285. Szeltner, Z, and Plogar, L. (1996), Conformational stability and catalytic activity of HIV 1 protcase are both enhanced at high salt concentration. Journal of Biological Chemistry. 271.5458-5463.
286. SZOSTAK, J.W. (1992). in vitro genetics. Trends in Biochemical Sciences. 17, 89-93.
287. TAKAHASHI, Y., TANAKA, K, MURAKAMI, M., KAWASAKI, Y., TATSUML K, and OKAI, H. (1995), Characteristics of lipase modified with water-soluble acylating reagents and its csterification ability. Biosciettce Biotechnology and Biochemistiy, 59. 809-812.
288. TAMAKOSHI, M., YAMAGISHL A, and OSHJMA, T. (1995), Screening of stable proteins in an extreme thermophiie. Thenmts thermophilus, Molecular Microbiology, 16, 1031-1036.
289. Taneja, S, and Ahmad, F. (1994), Increased thermal stability of proteins in the presence of amino acids. Biochemical Journal. 303, 147-153.
290. TANFORD, C. (1979), Interfacial free energy and the hydrophobic effcct. Proceedings of the National Academy of Science USA. 76, 4175-4176.
291. Tanner, J.J., Hecht, R.M, and Krause, K.L. (1996), Determinants of enzyme thermostability observed in the molecular structure of Thermits aquations D-glyceraldehyde-3-phosphate dehydrogenase at 2.5, A resolution. Biochemistiy, 35,2597-2609.
292. TATSIMOTO, K, Oh, K.K., BAKER, J.O, and HIMMEL, M.E. (1989), Enhanced stability of glucoamylase through chemical crosslinking. Applied Biochemistry and Biotechnology, 20/21, 293.
293. THOMAS, K.A., SMITH, G.M., THOMAS, T.B, and FELDMANN, R. J. (1982), Electronic distributions within protein phenylalanine aromatic rings are reflected by the three-dimensional oxygen atom environments. Proceedings of the National Academy of Science USA, 79, 4843-4847.
294. Tissot, A.C., VUILLEUMIER, S, and Fersht, A.R. (1996), Importance of two buried salt bridges in the stability and folding pathway of bamase. Biochemistiy, 35, 6786-6794.
295. TOMIZAWA, H., YAMADA, H., WADA, K, and IMOTO, T. (1995a), Stabilization of lysozyme against iircversible inactivation by suppression of chemical reacuons. Journal of Biochemistiy. 117, 635-640.
296. TOMIZAWA, H., YAMADA, H., HASHIMOTO, Y., and IMOTO, T. (1995b), Stabilization of lysozyme against irreversible inactivation by alteration of the Asp Gly sequences. Protein Engineering, S. 1023-1028.
297. TORCHILIN v.p., MAKSIMENKO A.V., SMIRNOV V.N., BEREZIN I.V., KLIBANOV A.M, and MARTI NEK, K. (1978), Hie principles of enzyme stabilization III: The effect of the length of intra-molecularcross-linkageson thermostability of enzymts, Biochemica and Biophvsica Acta. 522, 277-283.
298. Torchilin, V.P., Maksimenko, A. V., Smirnov, V.N., Berezin, L.N, Klibanov, A. M, and Martinek, K. (1979), The principles of enzyme stabilization: modification of key functional groups in the tertiary structure of proteins. Biochimica and Biophysica Acta, 567, 1-11.
299. Torchilin, V.P, and Martinek, K. (1979), Enzyme stabilization without carriers. Enzyme Microbial Technology. 1, 74-82.
300. TUENGLER P, and PFLEIDERER, G. (1977), Enhanced heat, alkaline and tryptic stability of acetamidinated pig heart lactate dehydrogenase. Biochirnica and Biophysica Acta, 484, 1-8.
301. Tyagi R, & GUPTA M.N. (1993). In: Thermostability of Enzymes. (Gupta, M.N, Gupta, Ed.), Springer-Verlag Narosa Publishing House, 146-160.
302. UEDA, T., IWASHITA, H., HASHIMOTO, Y, and IMOTO, T. (1996), Stabilization of lysozyme by introducing glycosylation signal sequence. Journal of Biochemistry, H9, 157-161.
303. ULBRICH HOFMANN, R., MANSFELD, J., FJ ITKAU, S., DAMERAU, W. (1995), Structural flexibility in extremely stable carrier-bound chymotrypsin. Biotechnology and Applied Biochemistry. 22, 75-94.
304. VAN BERKEL, P.H.C., GFERTS, M.E.J., VAN VEEN, H.A., LOOIMAN, P.M., PIEPER, F.R., DEBOER, H.A, and NUIJENS, J.H. (1995), Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial lipopolysaccharide, but differ in their susceptibilities towards tryptic proteolysis. Biochemical Journal, 312, 107-114.
305. VAN DEN BURG, B., DUKSTRA, B.W., VAN DER VINNE, B., VENEMA, G, and EIJSINK, V.G.H. (1994), Protein stabilization by hydrophobic interactions at the surface. European Journal of Biochemistry, 220, 981-985.
306. Vanhove, M., Houba, S., Lamotte-Brasseur, J, and Frere J.-M. (1995), Probing the determinants of protein stability: comparison of class A p-lactamases. Biochemical Journal, 308, 859-864.
307. VARSANI, L., CUL, T, RANGARAJAN, M., HARTLEY, B.S., GOLDBERG, J., COLLYER C, and BLOW, D.M. (1993). Arthrobacter D-xylose isomerase: protein-engineering subunit interfaces. Biochemical Journal, 291, 575-583.
308. VIGUERA, A.R, and Serrano, L. (1995), Side-chain interactions between sulfur-containing amino acids and phenylalanine in alpha-helices. Biochemistry, 34, 8771-8779.
309. VILLAFRANCA, J.E., HOWELL, E.E., VOET, D.H., STROBEL, M.S., OGDEN, R.L., ABELSON, J.N, and KRAUT, J. (1983), Directed mutagenesis of dihydropholate reductase. Science, 222, 782-788.
310. Volk, O., MARKIEWICZ, P., STETTER, K.O, and MILLER, J.H. (1994), The sequence of a subtilisin-type protease (aerolysin), from the hyperthermophilic archaeum Pyrobacuhtm aerophilum reveals sites important to thermostability. Protein Science, 3, 1329-1340.
311. WADA, A, and NaKumura, H. (1981), Nature of the charge distribution in proteins. Nature, 293,757-758.
312. Waldburger, C.D., Schildbach, J.F, and Sauer, R.T. (1995), Are buried salt bridges important for protein stability and conformation specificity. Nature Structural Biology, 2, 122-128.
313. Walsh, G, and Headon, D. (1994). In: Protein Biotechnology, John Willey and Sons Ltd, p.306.
314. WANG, C., EUFEMI, M., TURANO, C, and GIARTOSIO, A. (1996), Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry, 35,7299-7307.
315. WARD, O.P, and MOO-YOUNG, M. (1988). In: Biotechnology Advances (Moo-Young, M., Bu'Lock, J.D., Cooney, C.L. and Glick, B.R., eds), Pergamon, N.Y., Vol 6, 39-69.
316. Warren, G.L, and Petsko, G.A. (1995), Composition analysis of alpha helices in thermophilic organisms. Protein Engineering, 9, 905-913.
317. Wartchow, C.A., WANG, P., Bednarskind Callstrom, M.R. (1995), Carbohydrate pro- leaseconjugates: Stabilized proteasesforpeptide synhesh. Journal of Organic Chemistry. 60, 2216-2226.
318. WASSERMAN, B.P. (1984), Thermostable enzyme production. Food Technol, 38, 78.
319. WEGMANN, K. (1986), Osmoregulation in eucaryotic algae. FEMSMicrobiol, Review. 39, 37-43.
320. WELLS, J.A. (1990), Additivity of Mutational Effects in Proicms Biochemistry, 29,8509-8527.
321. Wetzel, R., perry, L.J., Baase, W. A, and BECKEL, J.W. (1988), Disulfide bonds and thermal stability in T4 lysozyme. Proceedings of the National Academy of Science USA, 85, 401-405.
322. Williams, G.A, MacEvilly, U., Ryan, R, and Harrington, M.G. (1995), Stabilization of ribonuclease B activity by concentrated xylose solutions. Biochemical and Biophysical Research Communications. 207,432-437.
323. WIMLEY, W., CREAMER, T.P, and WHITE, S.H. (1990), Solvation energies of amino acid side chains and backbone in a family of host-guesi pentapeptides. Biochemistry, 35, 5109-5124.
324. WISEMAN, A. (1983), Mechanisms of catalyses: opposing relationship with enzyme stability. Biochemical Society Transactions. 11, 1982-1983.
325. Wiss, D.F., CHOI, J.S, and WAGNER, G. (1995a), Composition and sequence specific resonance assignment of the heterogeneous N-linked glycan in the 13.6 kDa adhesion domain of human CD2 as determined by NMR on the intact glycoprotein. Biochemistry, 34, 1622-1634.
326. WISS, D.F., Choi, J.S, and WAGNER, G. (1995b), Conformation and function of N-linked glycan in the adhesion domain of human CD2. Science, 269, 1273-1278.
327. WOLFENDEN, B, and ERSSON, L, CULLIS, P.M, and SOUTHGATE, C-C-B. (1981), Affinities of amino acid side chains for solvent water. Biochemistry. 20, 849-855.
328. YAMASHITA, M., KINOSHITA, T., IHARA M., MIKAWA, T, and MUROOKA, Y. (1994), Random mutagenesis of pullulanase from Klebsiella aerogenes for studies of the structure and function of the enzyme. Journal of Biochemistiy. 116, 1233-1240.
329. YANCEY, P.H., CLARK, M.E., HAND, S.C., BOWLUS, R.D, and SOMERO, G.N. (1982), Living with water stress: evolution of osmolyte system. Science. 217, 1214-1222.
330. YANG, Z., WILLIAMS, D, and Russell, A. J. (1995a), Synthesis of protein-containing polymers in organic solvents. Biotechnology and Bioengineering. 45, 10-17.
331. YANG, Z., MESIANO, AJ., VENKATASUBRAMANIAN, S., GROSS, S.H., HARRIS, J.M, and RUSSELL, A.J. (1995b), Activity and stability of enzymes incorporated into acrylic polymers. Journal of the American Chemical Society. 117, 4843-4850.
332. YANG, Z., DOMACH, M., AUGER, R., YANG, F.X, and RUSSEL, A.J. (1996), Polyethylene glycol induced stabilization of subtilisin. Enzyme and Microbial Technology. 18,82-89.
333. Yu, M.-H., WEISSMAN, J.S, and KIM, P.S. (1995), Contribution of individual side-chains to the stability of BPT1 examined by alanine-scanning mutagenesis. Journal of Molecular Biology, 249, 388-397.
334. Yu, Y.H., MONERA, O.D., Hodges, R.S, and Privalov, P.L. (1996), ion pairs significantly stabilize coiled coils in the absencc of electrolyte. Journal of Molecular Biology, 255, 367-372.
335. Yumoto, N, Murase, S, Hattori, T, Yamamoto, H, Tatsu, Y., and Yoshikawa, S. (1993), Stabilization of a-helix in C-terminal fragments of neuropeptide Y. Biochemical and Biophysical Research Communications. 196, 1490-1495.
336. YUTANI, K., OGASAHARA, K., SUGINO, Y., and MATSUSHIRO, A. (1977), Effect of a single amino acid substitution on stability of conformation of a protein. Nature. 267, 274-275.
337. YUTANI, K., OGASAHARA, K., TSUJITA, T, and SUGINO, Y. (1987), Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase a subunit. Proceedings of the National Academy of Science USA. 84, 4441-4444.
338. ZABORSKY, O.R. (1973). In: Immobilized Enzymes, The Chemical Rubber co, Cranwood Parkway, Cleveland, Ohio, 44128.
339. ZUANG, T., BERTELSEN, E, and ALBER, T. (1994), Entropic effects of disulfide bonds on protein stability. Nature Structural Biology. 1, 434-438.
340. ZHANG, X.-J., BAASE, W.A, and MATTHEWS, B.W. (1992), Multiple alanine replacements within a-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. Protein Sci., 1, 761-776.
341. ZHANG, X.J., BAASE, W.A., SHOICHET, B.K., WILSON, K.P. (1995), Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. Protein Engineering. 8, 1017-1022.