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Volumn 7, Issue 11, 1998, Pages 2345-2353

Stabilizing the subtilisin BPN' pro-domain by phage display selection: How restrictive is the amino acid code for maximum protein stability?

Author keywords

Combinatorial genetics; Protein folding; Site directed mutagenesis; Stopped flow kinetics; Thermodynamics

Indexed keywords

MUTANT PROTEIN; SERINE PROTEINASE; SUBTILISIN;

EID: 0031733866     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071111     Document Type: Article
Times cited : (43)

References (38)
  • 1
    • 0026764471 scopus 로고
    • Thermodynamic analysis of the folding of the Streptococcal Protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures
    • Alexander P, Fahnestock S, Lee T, Orban J, Bryan P. 1992. Thermodynamic analysis of the folding of the Streptococcal Protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures. Biochemistry 31:3591-3603.
    • (1992) Biochemistry , vol.31 , pp. 3591-3603
    • Alexander, P.1    Fahnestock, S.2    Lee, T.3    Orban, J.4    Bryan, P.5
  • 3
    • 0027249641 scopus 로고
    • De novo protein design: From molten globules to native-like states
    • Betz SF, Raleigh DP, DeGrado WF. 1993. De novo protein design: From molten globules to native-like states. Curr Opin Struct Biol 3:601-610.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 601-610
    • Betz, S.F.1    Raleigh, D.P.2    DeGrado, W.F.3
  • 4
    • 0001059847 scopus 로고
    • Thermodynamics of protein denaturation. II. A model of reversible denaturation and interpretations regarding the stability of chymotrypsinogen
    • Brandts JF. 1964. Thermodynamics of protein denaturation. II. A model of reversible denaturation and interpretations regarding the stability of chymotrypsinogen. J Am Chem Soc 86:4302-4314.
    • (1964) J Am Chem Soc , vol.86 , pp. 4302-4314
    • Brandts, J.F.1
  • 8
    • 0028858499 scopus 로고
    • De novo design of the hydrophobic cores of proteins
    • Desjarlais JR, Handel TM. 1995. De novo design of the hydrophobic cores of proteins. Protein Sci 4:2006-2018.
    • (1995) Protein Sci , vol.4 , pp. 2006-2018
    • Desjarlais, J.R.1    Handel, T.M.2
  • 9
    • 0029645412 scopus 로고
    • The prosegment-subtilisin BPN′ complex: Crystal structure of a specific foldase
    • Gallagher TD, Gilliland G, Wang L, Bryan P. 1995. The prosegment-subtilisin BPN′ complex: Crystal structure of a specific foldase. Structure 3:907-914.
    • (1995) Structure , vol.3 , pp. 907-914
    • Gallagher, T.D.1    Gilliland, G.2    Wang, L.3    Bryan, P.4
  • 10
    • 0029958604 scopus 로고    scopus 로고
    • A test of the jigsaw puzzle model for protein folding by multiple methionine substitutions within the core of T4 lysozyme
    • Gassner NC, Baase WA, Matthews BW. 1996. A test of the jigsaw puzzle model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. Proc Natl Acad Sci USA 93:12155-12158.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12155-12158
    • Gassner, N.C.1    Baase, W.A.2    Matthews, B.W.3
  • 11
    • 0024385337 scopus 로고
    • Folding of a peptide corresponding to the alpha-helix in bovine pancreatic trypsin inhibitor
    • Goodman EM, Kim PS. 1989. Folding of a peptide corresponding to the alpha-helix in bovine pancreatic trypsin inhibitor. Biochemistry 28:4343-4347.
    • (1989) Biochemistry , vol.28 , pp. 4343-4347
    • Goodman, E.M.1    Kim, P.S.2
  • 12
    • 0029004982 scopus 로고
    • A phage display system for studying the sequence determinants of protein folding
    • Gu H, Qian Y, Bray ST, Riddle DS, Shiau AK, Baker D. 1995. A phage display system for studying the sequence determinants of protein folding. Protein Sci 4:1108-1117.
    • (1995) Protein Sci , vol.4 , pp. 1108-1117
    • Gu, H.1    Qian, Y.2    Bray, S.T.3    Riddle, D.S.4    Shiau, A.K.5    Baker, D.6
  • 13
    • 0026699293 scopus 로고
    • Selection of phage antibodies by binding affinity: Mimicking affinity maturation
    • Hawkins RE, Russell SJ, Winter G. 1992. Selection of phage antibodies by binding affinity: Mimicking affinity maturation. J Mol Biol 226:889-896.
    • (1992) J Mol Biol , vol.226 , pp. 889-896
    • Hawkins, R.E.1    Russell, S.J.2    Winter, G.3
  • 14
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom HR, Griffiths AD, Johnson KS, Chiswell DJ, Hudson P, Winter G. 1991. Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res 19:4133-4137.
    • (1991) Nucleic Acids Res , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 15
    • 0023644876 scopus 로고
    • Requirement of pro sequence for the production of active subtilisin in Escherichia coli
    • Ikemura H, Takagi H, Inouye M. 1987. Requirement of pro sequence for the production of active subtilisin in Escherichia coli. J Biol Chem 262:7859-7864.
    • (1987) J Biol Chem , vol.262 , pp. 7859-7864
    • Ikemura, H.1    Takagi, H.2    Inouye, M.3
  • 16
    • 23444436172 scopus 로고
    • Protein design by binary pattern of polar and nonpolar amino acids
    • Kamtekar S, Schiffer JM, Xiong H, Babik JM, Hecht MH. 1993. Protein design by binary pattern of polar and nonpolar amino acids. Science 262:1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.M.2    Xiong, H.3    Babik, J.M.4    Hecht, M.H.5
  • 18
    • 0024535615 scopus 로고
    • A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96 → His mutant form thereof
    • Kitamura S, Sturtevant JM. 1989. A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96 → His mutant form thereof. Biochemistry 28:3788-3792.
    • (1989) Biochemistry , vol.28 , pp. 3788-3792
    • Kitamura, S.1    Sturtevant, J.M.2
  • 19
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0028579713 scopus 로고
    • Different protein sequences can give rise to highly similar folds through different stabilizing interactions
    • Laurents DV, Subbiah S, Levitt M. 1994. Different protein sequences can give rise to highly similar folds through different stabilizing interactions. Protein Sci 3:1938-1944.
    • (1994) Protein Sci , vol.3 , pp. 1938-1944
    • Laurents, D.V.1    Subbiah, S.2    Levitt, M.3
  • 22
    • 0030992890 scopus 로고    scopus 로고
    • De novo design of the hydrophobic core of ubiquitin
    • Lazar GA, Desjarlais JR, Handel TM. 1997. De novo design of the hydrophobic core of ubiquitin. Protein Sci 6:1167-1178.
    • (1997) Protein Sci , vol.6 , pp. 1167-1178
    • Lazar, G.A.1    Desjarlais, J.R.2    Handel, T.M.3
  • 23
    • 0025908265 scopus 로고
    • The role of internal packing interactions in determining the structure and stability of a protein
    • Lim WA, Sauer RT. 1991. The role of internal packing interactions in determining the structure and stability of a protein. J Mol Biol 219:359-376.
    • (1991) J Mol Biol , vol.219 , pp. 359-376
    • Lim, W.A.1    Sauer, R.T.2
  • 25
    • 0000295996 scopus 로고
    • Secretion and autoproteolytic maturation of subtilisin
    • Power SD, Adams RM, Wells JA. 1986. Secretion and autoproteolytic maturation of subtilisin. Proc Natl Acad Sci USA 83:3096-3100.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3096-3100
    • Power, S.D.1    Adams, R.M.2    Wells, J.A.3
  • 26
    • 0018588511 scopus 로고
    • Stability of proteins small globular proteins
    • Privalov PL. 1979. Stability of proteins small globular proteins. Adv Protein Chem 33:167-241.
    • (1979) Adv Protein Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 27
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov PL, Khechinashvili NN. 1974. A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study. J Mol Biol 86:665-684.
    • (1974) J Mol Biol , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 28
    • 0023949179 scopus 로고
    • Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences
    • Reidhaar-Olson JF, Sauer RT. 1988. Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences. Science 241:53-57.
    • (1988) Science , vol.241 , pp. 53-57
    • Reidhaar-Olson, J.F.1    Sauer, R.T.2
  • 29
    • 0030878180 scopus 로고    scopus 로고
    • A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties
    • Roy S, Ratnaswamy G, Boice JA, Fairman R, McLendon G, Hecht MH. 1997. A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties. J Am Chem Soc 119:5302-5306.
    • (1997) J Am Chem Soc , vol.119 , pp. 5302-5306
    • Roy, S.1    Ratnaswamy, G.2    Boice, J.A.3    Fairman, R.4    McLendon, G.5    Hecht, M.H.6
  • 30
    • 0030803268 scopus 로고    scopus 로고
    • Engineering the independent folding of the subtilisin BPN′ pro-domain: Analysis of two-state folding vs. protein stability
    • Ruvinov S, Wang L, Ruan B, Almog O, Gilliland G. Eisenstein E, Bryan P. 1997. Engineering the independent folding of the subtilisin BPN′ pro-domain: Analysis of two-state folding vs. protein stability. Biochemistry 36:10414-10421.
    • (1997) Biochemistry , vol.36 , pp. 10414-10421
    • Ruvinov, S.1    Wang, L.2    Ruan, B.3    Almog, O.4    Gilliland, G.5    Eisenstein, E.6    Bryan, P.7
  • 31
    • 0002983608 scopus 로고    scopus 로고
    • Protein folding from a combinatorial perspective
    • Sauer RT. 1996. Protein folding from a combinatorial perspective. Fold Design 1:27-30.
    • (1996) Fold Design , vol.1 , pp. 27-30
    • Sauer, R.T.1
  • 32
    • 0027266779 scopus 로고
    • Libraries of peptides displayed on filamentous phage
    • Smith GP, Scott JK. 1993. Libraries of peptides displayed on filamentous phage. Methods Enzym 217:228-257.
    • (1993) Methods Enzym , vol.217 , pp. 228-257
    • Smith, G.P.1    Scott, J.K.2
  • 33
    • 0027244542 scopus 로고
    • Catalysis of a protein folding reaction: Thermodynamic and kinetic analysis of subtilisin BPN′ interactions with its propeptide fragment
    • Strausberg S, Alexander P, Wang L, Schwarz F, Bryan P. 1993. Catalysis of a protein folding reaction: Thermodynamic and kinetic analysis of subtilisin BPN′ interactions with its propeptide fragment. Biochemistry 32:8112-8119.
    • (1993) Biochemistry , vol.32 , pp. 8112-8119
    • Strausberg, S.1    Alexander, P.2    Wang, L.3    Schwarz, F.4    Bryan, P.5
  • 34
    • 0021127425 scopus 로고
    • Genes for alkaline and neutral protease from Bacillus amyloliquifaciens contain a large open-reading frame between the regions coding for signal sequence and mature protein
    • Vasantha N, Thompson LD, Rhodes C, Banner C, Nagle J, Filpula D. 1984. Genes for alkaline and neutral protease from Bacillus amyloliquifaciens contain a large open-reading frame between the regions coding for signal sequence and mature protein. J Bacteriol 159:811-819.
    • (1984) J Bacteriol , vol.159 , pp. 811-819
    • Vasantha, N.1    Thompson, L.D.2    Rhodes, C.3    Banner, C.4    Nagle, J.5    Filpula, D.6
  • 35
    • 0032478201 scopus 로고    scopus 로고
    • Engineering the independent folding of the subtilisin BPN′ pro-domain: Correlation of pro-domain stability with the rate of subtilisin folding
    • Wang L, Ruan B, Ruvinov S, Bryan PN. 1998. Engineering the independent folding of the subtilisin BPN′ pro-domain: Correlation of pro-domain stability with the rate of subtilisin folding. Biochemistry 37:3165-3171.
    • (1998) Biochemistry , vol.37 , pp. 3165-3171
    • Wang, L.1    Ruan, B.2    Ruvinov, S.3    Bryan, P.N.4
  • 36
    • 0028973036 scopus 로고
    • Prodomain mutations at the subtilisin interface: Correlation of binding energy and the rate of catalyzed folding
    • Wang L, Ruvinov S, Strausberg S, Gallagher TD, Gilliland G, Bryan P. 1995. Prodomain mutations at the subtilisin interface: Correlation of binding energy and the rate of catalyzed folding. Biochemistry 34:15415-15420.
    • (1995) Biochemistry , vol.34 , pp. 15415-15420
    • Wang, L.1    Ruvinov, S.2    Strausberg, S.3    Gallagher, T.D.4    Gilliland, G.5    Bryan, P.6
  • 37
    • 0021112782 scopus 로고
    • Cloning sequencing and secretion of Bacillus amyloliquifaciens subtilisin in Bacillus subtilis
    • Wells JA, Ferrari E, Henner DJ, Estell DA, Chen EY. 1983. Cloning sequencing and secretion of Bacillus amyloliquifaciens subtilisin in Bacillus subtilis. Nucleic Acids Res 11:7911-7925.
    • (1983) Nucleic Acids Res , vol.11 , pp. 7911-7925
    • Wells, J.A.1    Ferrari, E.2    Henner, D.J.3    Estell, D.A.4    Chen, E.Y.5
  • 38
    • 0028846974 scopus 로고
    • Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins
    • West MW, Hecht MH. 1995. Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins. Protein Sci 4:2032-2039.
    • (1995) Protein Sci , vol.4 , pp. 2032-2039
    • West, M.W.1    Hecht, M.H.2


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