메뉴 건너뛰기




Volumn 257, Issue 5, 1996, Pages 1112-1126

Stability changes upon mutation of solvent-accessible residues in proteins evaluated by database-derived potentials

Author keywords

Backbone torsion potentials; Folding free energies; Protein stability; Residue residue interaction potentials; Single site mutations

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; BACTERIOPHAGE T4; DATA BASE; ELECTRIC ACTIVITY; IONIC STRENGTH; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; SEQUENCE ANALYSIS;

EID: 0029873155     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0226     Document Type: Article
Times cited : (141)

References (57)
  • 2
    • 0023346161 scopus 로고
    • Free energy calculations by computer simulation
    • Basch, P. A., Singh, U. C., Langridge, R. & Kollman, P. A. (1987). Free energy calculations by computer simulation. Science, 236, 564-568.
    • (1987) Science , vol.236 , pp. 564-568
    • Basch, P.A.1    Singh, U.C.2    Langridge, R.3    Kollman, P.A.4
  • 4
    • 0027236794 scopus 로고
    • Structural basis of amino acid a helix propensity
    • Blaber, M., Zang, X. & Matthews, B. W. (1993). Structural basis of amino acid a helix propensity. Science, 260, 1637-1640.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zang, X.2    Matthews, B.W.3
  • 5
    • 0027318317 scopus 로고
    • An empirical energy function for threading protein sequence through folding motif
    • Bryant, S. H. & Lawrence, C. E. (1993). An empirical energy function for threading protein sequence through folding motif. Proteins: Struct. Funct. Genet. 16, 92-112.
    • (1993) Proteins: Struct. Funct. Genet. , vol.16 , pp. 92-112
    • Bryant, S.H.1    Lawrence, C.E.2
  • 6
    • 0026539511 scopus 로고
    • Structure-derived hydrophobic potential. Hydrophobic potential derived from X-ray structures of globular proteins is able to identify native folds
    • Casari, G. & Sippl, M. J. (1992). Structure-derived hydrophobic potential. Hydrophobic potential derived from X-ray structures of globular proteins is able to identify native folds. J. Mol. Biol. 224, 725-732.
    • (1992) J. Mol. Biol. , vol.224 , pp. 725-732
    • Casari, G.1    Sippl, M.J.2
  • 7
    • 0024442265 scopus 로고
    • Free energy calculations on protein stability: Thr157 → Val157 mutation of T4 lysozyme
    • Dang, L. X., Merz, K. M., Jr & Kollman, P. A. (1989). Free energy calculations on protein stability: Thr157 → Val157 mutation of T4 lysozyme. J. Am. Chem. Soc. 111, 8505-8508.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8505-8508
    • Dang, L.X.1    Merz K.M., Jr.2    Kollman, P.A.3
  • 8
    • 0025321279 scopus 로고
    • A mutant T4 lysozyme (Val131 → Ala) designed to increase thermostability by the reduction of strain within an α-helix
    • Dao-Pin, S., Baase, W. A. & Matthews, B. W. (1990). A mutant T4 lysozyme (Val131 → Ala) designed to increase thermostability by the reduction of strain within an α-helix. Proteins: Struct. Funct. Genet. 7, 198-204.
    • (1990) Proteins: Struct. Funct. Genet. , vol.7 , pp. 198-204
    • Dao-Pin, S.1    Baase, W.A.2    Matthews, B.W.3
  • 9
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • Eriksson, A. E., Baase, W. A., Zhang X.-J., 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.
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Baase, W.A.2    Zhang, X.-J.3    Heinz, D.W.4    Blaber, M.5    Baldwin, E.P.6    Matthews, B.W.7
  • 10
    • 0027462173 scopus 로고
    • Principles of protein stability derived from protein engineering exper-iments
    • Fersht, A. R. & Serrano, L. (1993). Principles of protein stability derived from protein engineering exper-iments. Curr. Opin. Struct. Biol. 3, 75-83.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 75-83
    • Fersht, A.R.1    Serrano, L.2
  • 12
    • 0026755510 scopus 로고
    • Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: Evidence for mutational effects on the free energy of the denatured state
    • Green, S. M., Meeker, A. K. & Shortle, D. (1992). Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. Biochemistry, 31, 5717-5728.
    • (1992) Biochemistry , vol.31 , pp. 5717-5728
    • Green, S.M.1    Meeker, A.K.2    Shortle, D.3
  • 13
    • 0026674251 scopus 로고
    • α-Helix stability in proteins. II. Factors that influence stability at an internal position
    • Horovitz, A., Matthews, J. M. & Fersht, A. R. (1992). α-Helix stability in proteins. II. Factors that influence stability at an internal position. J. Mol. Biol. 227, 560-568.
    • (1992) J. Mol. Biol. , vol.227 , pp. 560-568
    • Horovitz, A.1    Matthews, J.M.2    Fersht, A.R.3
  • 14
    • 0026516391 scopus 로고
    • Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme
    • Hu, C.-Q., Kitamura, S., Tanaka, A. & Sturtevant, J. M. (1992). Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. Biochemistry, 31, 1643-1647.
    • (1992) Biochemistry , vol.31 , pp. 1643-1647
    • Hu, C.-Q.1    Kitamura, S.2    Tanaka, A.3    Sturtevant, J.M.4
  • 15
    • 0025744921 scopus 로고
    • SESAM, a relational database for structure and sequence of macromolecules
    • Huysmans, M., Richelle, J. & Wodak, S. J. (1991). SESAM, a relational database for structure and sequence of macromolecules. Proteins: Struct. Funct. Genet. 11, 59-76.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 59-76
    • Huysmans, M.1    Richelle, J.2    Wodak, S.J.3
  • 16
    • 0028174179 scopus 로고
    • Engineering alternative β-turn types in staphylococcal nuclease
    • Hynes, T. R., Hodel, A. & Fox, R. O. (1994). Engineering alternative β-turn types in staphylococcal nuclease. Biochemistry, 3, 5021-5030.
    • (1994) Biochemistry , vol.3 , pp. 5021-5030
    • Hynes, T.R.1    Hodel, A.2    Fox, R.O.3
  • 17
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254, 260-288.
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 18
    • 0027959459 scopus 로고
    • Contribution of residues in the reactive site loop of chymotrypin inhibitor 2 to protein stability and activity
    • Jackson, S. E. & Fersht, A. R. (1994). Contribution of residues in the reactive site loop of chymotrypin inhibitor 2 to protein stability and activity. Biochemistry, 33, 13880-13887.
    • (1994) Biochemistry , vol.33 , pp. 13880-13887
    • Jackson, S.E.1    Fersht, A.R.2
  • 19
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 20
    • 0024375463 scopus 로고
    • Energetics of complementary side-chain packing in a protein hydrophobic core
    • Kellis, J. T., Jr, Nyberg, K. & Fersht, A. R. (1989). Energetics of complementary side-chain packing in a protein hydrophobic core. Biochemistry, 28, 4914-4922.
    • (1989) Biochemistry , vol.28 , pp. 4914-4922
    • Kellis J.T., Jr.1    Nyberg, K.2    Fersht, A.R.3
  • 21
    • 0028318094 scopus 로고
    • Factors influencing the ability of knowledge-based potentials to identify native sequence-structure matches
    • Kocher, J.-P. A., Rooman, M. J. & Wodak, S. J. (1994). Factors influencing the ability of knowledge-based potentials to identify native sequence-structure matches. J. Mol. Biol. 235, 1598-1613.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1598-1613
    • Kocher, J.-P.A.1    Rooman, M.J.2    Wodak, S.J.3
  • 22
    • 0028063257 scopus 로고
    • Polar and nonpolar atomic environments in the protein core: Implications for folding and binding
    • Koehl, P. & Delarue, M. (1994). Polar and nonpolar atomic environments in the protein core: implications for folding and binding. Proteins: Struct. Funct. Genet. 20, 264-278.
    • (1994) Proteins: Struct. Funct. Genet. , vol.20 , pp. 264-278
    • Koehl, P.1    Delarue, M.2
  • 23
    • 0028223845 scopus 로고
    • Predicting protein mutant energetics by self-consistent ensemble optimization
    • Lee, C. (1994). Predicting protein mutant energetics by self-consistent ensemble optimization. J. Mol. Biol. 236, 918-939.
    • (1994) J. Mol. Biol. , vol.236 , pp. 918-939
    • Lee, C.1
  • 24
    • 0026210071 scopus 로고
    • Accurate prediction of the stability and activity effects on site-directed mutagenesis on a protein core
    • Lee, C. & Levitt, M. (1991). Accurate prediction of the stability and activity effects on site-directed mutagenesis on a protein core. Nature, 352, 448-451.
    • (1991) Nature , vol.352 , pp. 448-451
    • Lee, C.1    Levitt, M.2
  • 25
    • 0029082531 scopus 로고
    • Empirical correlation for the replacement of ala by gly: Importance of amino acid secondary intrinsic propensities
    • López-Hernández, E. & Serrano, L. (1995). Empirical correlation for the replacement of ala by gly: importance of amino acid secondary intrinsic propensities. Proteins: Struct. Funct. Genet. 22, 340-349.
    • (1995) Proteins: Struct. Funct. Genet. , vol.22 , pp. 340-349
    • López-Hernández, E.1    Serrano, L.2
  • 26
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matoushek, A., Kellis, J. T., Jr, Serrano, L. & Fersht, A. R. (1989). Mapping the transition state and pathway of protein folding by protein engineering. Nature, 340, 122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matoushek, A.1    Kellis J.T., Jr.2    Serrano, L.3    Fersht, A.R.4
  • 27
    • 0027998757 scopus 로고
    • Context is a major determinant of β-sheet propensity
    • Minor, D., Jr & Kim, P. S. (1994). Context is a major determinant of β-sheet propensity. Nature, 371, 264-267.
    • (1994) Nature , vol.371 , pp. 264-267
    • Minor D., Jr.1    Kim, P.S.2
  • 28
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures
    • Miyazawa, S. & Jernigan, R. L. (1985). Estimation of effective interresidue contact energies from protein crystal structures. Macromolecules, 18, 534-552.
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 29
    • 0028075953 scopus 로고
    • Protein stability for single substitution mutants and the extent of local compactness in the denatured state
    • Miyazawa, S. & Jernigan, R. L. (1994). Protein stability for single substitution mutants and the extent of local compactness in the denatured state. Protein Eng. 7, 1209-1220.
    • (1994) Protein Eng. , vol.7 , pp. 1209-1220
    • Miyazawa, S.1    Jernigan, R.L.2
  • 30
    • 0028568650 scopus 로고
    • Intrinsic secondary structure propensities of the amino acids, using statistical f-y matrices: Comparison with experimental data
    • Muñoz, V. & Serrano, L. (1994). Intrinsic secondary structure propensities of the amino acids, using statistical f-y matrices: comparison with experimental data. Proteins: Struct. Funct. Genet. 20, 301-311.
    • (1994) Proteins: Struct. Funct. Genet. , vol.20 , pp. 301-311
    • Muñoz, V.1    Serrano, L.2
  • 31
    • 0028176281 scopus 로고
    • Kinetic characterization of the chemotactic protein from escherichia coli, CheY. Kinetic analysis of the inverse hydrophobic effect
    • Muñoz, V., López, E. M., Jager, M. & Serrano, L. (1994). Kinetic characterization of the chemotactic protein from escherichia coli, CheY. Kinetic analysis of the inverse hydrophobic effect. Biochemistry, 3, 5858-5866.
    • (1994) Biochemistry , vol.3 , pp. 5858-5866
    • Muñoz, V.1    López, E.M.2    Jager, M.3    Serrano, L.4
  • 32
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale
    • Nozaki, Y. & Tanford, C. (1971). The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J. Biol. Chem. 246, 2211-2217.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2
  • 33
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K. T. & DeGrado, W. F. (1990). A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science, 250, 646-650.
    • (1990) Science , vol.250 , pp. 646-650
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 34
    • 0023404610 scopus 로고
    • Proline-induced constraints in α-helices
    • Piela, L., Nemethy, G. N. & Scheraga, H. A. (1987). Proline-induced constraints in α-helices. Biopolymers, 26, 1587-1600.
    • (1987) Biopolymers , vol.26 , pp. 1587-1600
    • Piela, L.1    Nemethy, G.N.2    Scheraga, H.A.3
  • 35
    • 0015244817 scopus 로고
    • Empirical protein energy maps
    • Pohl, F. M. (1971). Empirical protein energy maps. Nature New Biol. 237, 277-279.
    • (1971) Nature New Biol. , vol.237 , pp. 277-279
    • Pohl, F.M.1
  • 37
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of a helices
    • Richardson, J. S. & Richardson, D. C. (1988). Amino acid preferences for specific locations at the ends of a helices. Science, 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 38
    • 0026458189 scopus 로고
    • Extracting information on folding from the amino acid sequence: Role of consensus stable regions in homologous proteins
    • Rooman, M. J. & Wodak, S. J. (1992). Extracting information on folding from the amino acid sequence: role of consensus stable regions in homologous proteins. Biochemistry, 31, 10239-10249.
    • (1992) Biochemistry , vol.31 , pp. 10239-10249
    • Rooman, M.J.1    Wodak, S.J.2
  • 39
    • 0029563695 scopus 로고
    • Are database-derived potentials valid for scoring both forward and inverted protein folding?
    • Rooman, M. J. & Wodak, S. J. (1995). Are database-derived potentials valid for scoring both forward and inverted protein folding? Protein Eng. 8, 849-858.
    • (1995) Protein Eng. , vol.8 , pp. 849-858
    • Rooman, M.J.1    Wodak, S.J.2
  • 40
    • 0026009212 scopus 로고
    • Prediction of protein backbone conformation based on 7 structure assignments: Influence of local interactions
    • Rooman, M. J., Kocher, J.-P. A. & Wodak, S. J. (1991). Prediction of protein backbone conformation based on 7 structure assignments: influence of local interactions. J. Mol. Biol. 221, 961-979.
    • (1991) J. Mol. Biol. , vol.221 , pp. 961-979
    • Rooman, M.J.1    Kocher, J.-P.A.2    Wodak, S.J.3
  • 41
    • 0026447086 scopus 로고
    • Extracting information on folding from the amino acid sequence: Accurate predictions for protein regions with stable conformation in absence of tertiary interactions
    • Rooman, M. J., Kocher, J.-P. A. & Wodak, S. J. (1992). Extracting information on folding from the amino acid sequence: accurate predictions for protein regions with stable conformation in absence of tertiary interactions. Biochemistry, 31, 10226-10238.
    • (1992) Biochemistry , vol.31 , pp. 10226-10238
    • Rooman, M.J.1    Kocher, J.-P.A.2    Wodak, S.J.3
  • 42
    • 0022412192 scopus 로고
    • Hydrophobicity of amino acid residues in globular proteins
    • Rose, G. D., Geselowitz, A. R., Lesser, G. J., Lee, R. H. & Zehfus, M. H. (1985). Hydrophobicity of amino acid residues in globular proteins. Science, 29, 834-838.
    • (1985) Science , vol.29 , pp. 834-838
    • Rose, G.D.1    Geselowitz, A.R.2    Lesser, G.J.3    Lee, R.H.4    Zehfus, M.H.5
  • 43
    • 0025911856 scopus 로고
    • Surface electrostatic interactions contribute little to stability of barnase
    • Sali, D., Bycroft, M. & Fersht, A. R. (1991). Surface electrostatic interactions contribute little to stability of barnase. J. Mol. Biol. 220, 779-788.
    • (1991) J. Mol. Biol. , vol.220 , pp. 779-788
    • Sali, D.1    Bycroft, M.2    Fersht, A.R.3
  • 44
    • 0025093185 scopus 로고
    • Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles
    • Serrano, L., Horovitz, A., Avron, B., Bycroft, M. & Fersht A. R. (1990). Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. Biochemistry, 29, 9343-9352.
    • (1990) Biochemistry , vol.29 , pp. 9343-9352
    • Serrano, L.1    Horovitz, A.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 45
    • 0026709329 scopus 로고
    • α-Helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces
    • Serrano, L., Sancho J., Hirshberg, M. & Fersht, A. R. (1992a). α-Helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. J. Mol. Biol. 227, 544-559.
    • (1992) J. Mol. Biol. , vol.227 , pp. 544-559
    • Serrano, L.1    Sancho, J.2    Hirshberg, M.3    Fersht, A.R.4
  • 46
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano, L., Kellis, J. T., Jr, Cann, P., Matouschek, A. & Fersht, A. R. (1992b). The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. J. Mol. Biol. 224, 783-804.
    • (1992) J. Mol. Biol. , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis J.T., Jr.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 48
    • 0025005525 scopus 로고
    • Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease
    • Shortle, D., Stites, W. E. & Meeker, A. K. (1990). Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. Biochemistry, 29, 8033-8041.
    • (1990) Biochemistry , vol.29 , pp. 8033-8041
    • Shortle, D.1    Stites, W.E.2    Meeker, A.K.3
  • 49
    • 0025341310 scopus 로고
    • Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge based prediction of local structures in globular proteins
    • Sippl, M. J. (1990). Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge based prediction of local structures in globular proteins. J. Mol. Biol. 213, 859-883.
    • (1990) J. Mol. Biol. , vol.213 , pp. 859-883
    • Sippl, M.J.1
  • 50
    • 0027650879 scopus 로고
    • Boltzmann's principle, knowledge-based mean fields and protein folding, An approach to the computational determination of protein structures
    • Sippl, M. J. (1993). Boltzmann's principle, knowledge-based mean fields and protein folding, An approach to the computational determination of protein structures. J. Comp. Aided Mol. Design 7, 473-501.
    • (1993) J. Comp. Aided Mol. Design , vol.7 , pp. 473-501
    • Sippl, M.J.1
  • 51
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl, M. J. (1995). Knowledge-based potentials for proteins. Curr. Opin. Struct. Biol. 5, 229-235.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 229-235
    • Sippl, M.J.1
  • 52
    • 0025732376 scopus 로고
    • Simulation analysis of the stability mutant R96H of T4 lysozyme
    • Tidor, B. & Karplus, M. (1991). Simulation analysis of the stability mutant R96H of T4 lysozyme. Biochemistry, 30, 3217-3228.
    • (1991) Biochemistry , vol.30 , pp. 3217-3228
    • Tidor, B.1    Karplus, M.2
  • 53
    • 0026669807 scopus 로고
    • Prediction of the activity and stability effects of site-directed mutagenesis on a protein core
    • van Gunsteren, W. F. & Mark, A. E. (1992). Prediction of the activity and stability effects of site-directed mutagenesis on a protein core. J. Mol. Biol. 227, 389-395.
    • (1992) J. Mol. Biol. , vol.227 , pp. 389-395
    • Gunsteren, W.F.1    Mark, A.E.2
  • 54
    • 0029863769 scopus 로고    scopus 로고
    • Automatic classification and analysis of αα-turn motifs in proteins
    • Wintjens, R. T., Rooman, M. J. & Wodak, S. J. (1996). Automatic classification and analysis of αα-turn motifs in proteins. J. Mol. Biol. 255, 235-253.
    • (1996) J. Mol. Biol. , vol.255 , pp. 235-253
    • Wintjens, R.T.1    Rooman, M.J.2    Wodak, S.J.3
  • 56
    • 0023368698 scopus 로고
    • 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 α-unit
    • Yutani, K., Ogasahara, K., Tsujita, T. & 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 α-unit. Proc. Natl Acad. Sci. USA, 84, 4441-4444.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4441-4444
    • Yutani, K.1    Ogasahara, K.2    Tsujita, T.3    Sugino, Y.4
  • 57
    • 0029585945 scopus 로고
    • Enhancement of protein stability by the combination of point mutation in T4 lysozyme is additive
    • Zhang, X., Baase, W. A., Shoichet, B. K., Wilson, K. P. & Matthews, B. W. (1995). Enhancement of protein stability by the combination of point mutation in T4 lysozyme is additive. Protein Eng. 8, 1017-1022.
    • (1995) Protein Eng. , vol.8 , pp. 1017-1022
    • Zhang, X.1    Baase, W.A.2    Shoichet, B.K.3    Wilson, K.P.4    Matthews, B.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.