메뉴 건너뛰기




Volumn 280, Issue 4, 1998, Pages 749-761

A general rule for the relationship between hydrophobic effect and conformational stability of a protein: Stability and structure of a series of hydrophobic mutants of human lysozyme

Author keywords

Disulfide bond; Double mutant; Human lysozyme; Hydrophobic effect; Protein stability

Indexed keywords

ALANINE; CYSTEINE; ISOLEUCINE; LYSOZYME; VALINE;

EID: 0032563127     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1906     Document Type: Article
Times cited : (63)

References (35)
  • 1
    • 0029892667 scopus 로고    scopus 로고
    • Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme
    • Baldwin, E., Xu, J., Hajiseyedjavadi, O., Baase, W. A. & Matthews, R. W. (1996). Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. J. Mol. Biol. 259, 542-559.
    • (1996) J. Mol. Biol. , vol.259 , pp. 542-559
    • Baldwin, E.1    Xu, J.2    Hajiseyedjavadi, O.3    Baase, W.A.4    Matthews, R.W.5
  • 3
    • 0027133653 scopus 로고
    • Crystal structural analysis of mutations in hydrophobic cores of barnase
    • Buckle, A. M., Henrick, K. & Fersht, A. R. (1993). Crystal structural analysis of mutations in hydrophobic cores of barnase. J. Mol. Biol. 234, 847-860.
    • (1993) J. Mol. Biol. , vol.234 , pp. 847-860
    • Buckle, A.M.1    Henrick, K.2    Fersht, A.R.3
  • 4
    • 0029882171 scopus 로고    scopus 로고
    • Structural and energetic responses to cavity-creating mutations in hydrophobic cores: Observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities
    • Buckle, A. M., Cramer, P. & Fersht, A. R. (1996). Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry, 35, 4298-4305.
    • (1996) Biochemistry , vol.35 , pp. 4298-4305
    • Buckle, A.M.1    Cramer, P.2    Fersht, A.R.3
  • 5
    • 0016352763 scopus 로고
    • Hydrophobic bonding and accessible surface area in proteins
    • Chothia, C. (1974). Hydrophobic bonding and accessible surface area in proteins. Nature, 248, 338-339.
    • (1974) Nature , vol.248 , pp. 338-339
    • Chothia, C.1
  • 6
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P. Y. & Fasman, G. D. (1978). Prediction of the secondary structure of proteins from their amino acid sequence. Advan. Enzymol. 47, 45-148.
    • (1978) Advan. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 7
    • 0027159949 scopus 로고
    • The molecular surface package
    • Connolly, M. L. (1993). The molecular surface package. J. Mol. Graph. 11, 139-141.
    • (1993) J. Mol. Graph. , vol.11 , pp. 139-141
    • Connolly, M.L.1
  • 8
    • 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
  • 9
    • 0027394606 scopus 로고
    • Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences
    • Eriksson, A. E., Baase, W. A. & Matthews, B. W. (1993). Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. J. Mol. Biol. 229, 747-769.
    • (1993) J. Mol. Biol. , vol.229 , pp. 747-769
    • Eriksson, A.E.1    Baase, W.A.2    Matthews, B.W.3
  • 10
    • 0011930746 scopus 로고
    • Theory of hydrophobic bonding. II. the correlation of hydrocarbon solubility in water with solvent cavity surface area
    • Hermann, R. B. (1972). Theory of hydrophobic bonding. II. The correlation of hydrocarbon solubility in water with solvent cavity surface area. J. Phys. Chem. 76, 2754-2759.
    • (1972) J. Phys. Chem. , vol.76 , pp. 2754-2759
    • Hermann, R.B.1
  • 11
    • 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
  • 12
    • 0025862426 scopus 로고
    • The crystal structure of a mutant human lysozyme C77/95a with increased secretion efficiency in yeast
    • Inaka, K., Taniyama, Y., Kikuchi, M., Morikawa, K. & Matsushima, M. (1991). The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast. J. Biol. Chem. 266, 12599-12603.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12599-12603
    • Inaka, K.1    Taniyama, Y.2    Kikuchi, M.3    Morikawa, K.4    Matsushima, M.5
  • 14
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann, W. (1959). Some factors in the interpretation of protein denaturation. Advan. Protein Chem. 14, 1-63.
    • (1959) Advan. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 15
    • 0024295240 scopus 로고
    • Contribution of hydrophobic interactions to protein stability
    • Kellis, J. T., Nyberg, K., Sali, D. & Fersht, A. R. (1988). Contribution of hydrophobic interactions to protein stability. Nature, 333, 784-786.
    • (1988) Nature , vol.333 , pp. 784-786
    • Kellis, J.T.1    Nyberg, K.2    Sali, D.3    Fersht, A.R.4
  • 16
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 17
    • 0026666598 scopus 로고
    • Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge cystein-77 and cystein-95
    • Kuroki, R., Inaka, K., Taniyama, Y., Kidokoro, S., Matsushima, M., Kikuchi, M. & Yutani, K. (1992). Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge cystein-77 and cystein-95. Biochemistry, 31, 8323-8328.
    • (1992) Biochemistry , vol.31 , pp. 8323-8328
    • Kuroki, R.1    Inaka, K.2    Taniyama, Y.3    Kidokoro, S.4    Matsushima, M.5    Kikuchi, M.6    Yutani, K.7
  • 18
    • 0023741058 scopus 로고
    • Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile3
    • Matsumura, M., Becktel, W. J. & Matthews, B. W. (1988). Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile3. Nature, 334, 406-410.
    • (1988) Nature , vol.334 , pp. 406-410
    • Matsumura, M.1    Becktel, W.J.2    Matthews, B.W.3
  • 19
    • 0030904568 scopus 로고    scopus 로고
    • A direct comparison of helix propensity in proteins and peptides
    • Myers, J. K., Pace, C. N. & Scholtz, J. M. (1997a). A direct comparison of helix propensity in proteins and peptides. Proc. Natl Acad. Sci. USA, 94, 2833-2837.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2833-2837
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 20
    • 0030858237 scopus 로고    scopus 로고
    • Helix propensities are identical in protein and peptides
    • Myers, J. K., Pace, C. N. & Scholtz, J. M. (1997b). Helix propensities are identical in protein and peptides. Biochemistry, 36, 10923-10929.
    • (1997) Biochemistry , vol.36 , pp. 10923-10929
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 21
    • 0027349239 scopus 로고
    • Hydration and heat stability effects on protein unfolding
    • Oobatake, M. & Ooi, T. (1993). Hydration and heat stability effects on protein unfolding. Prog. Biophys. Mol. Biol. 59, 237-284.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 237-284
    • Oobatake, M.1    Ooi, T.2
  • 22
    • 0027249564 scopus 로고
    • Residue helix parameters obtained from dichroic analysis of peptides of defined sequence
    • Park, S. H., Shalongo, W. & Stellwagen, E. (1993). Residue helix parameters obtained from dichroic analysis of peptides of defined sequence. Biochemistry, 32, 7048-7053.
    • (1993) Biochemistry , vol.32 , pp. 7048-7053
    • Park, S.H.1    Shalongo, W.2    Stellwagen, E.3
  • 23
  • 24
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov, P. L. & Khechinashvili, N. N. (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
  • 25
    • 0000398347 scopus 로고
    • Empirical correlation between hydrophobic free energy and aqueous cavity surface area
    • Reynolds, J. A., Gilbert, D. B. & Tanford, C. (1974). Empirical correlation between hydrophobic free energy and aqueous cavity surface area. Proc. Natl Acad. Sci. USA, 71, 2925-2927.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 2925-2927
    • Reynolds, J.A.1    Gilbert, D.B.2    Tanford, C.3
  • 26
    • 0030447864 scopus 로고    scopus 로고
    • Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol
    • Rohl, C. A., Chakrabartty, A. & Baldwin, R. L. (1996). Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Sci. 5, 2623-2637.
    • (1996) Protein Sci. , vol.5 , pp. 2623-2637
    • Rohl, C.A.1    Chakrabartty, A.2    Baldwin, R.L.3
  • 28
    • 0344382128 scopus 로고
    • Contribution of the large hydrophobic amino acids to the stability of staphylococcal nuclease
    • Shortle, D., Stites, W. E. & Meeker, A. K. (1990). Contribution of the large hydrophobic amino acids to the stability of staphylococcal nuclease. Biochemistry, 30, 9686-9697.
    • (1990) Biochemistry , vol.30 , pp. 9686-9697
    • Shortle, D.1    Stites, W.E.2    Meeker, A.K.3
  • 29
    • 0028786432 scopus 로고
    • Contribution of hydrophobic residues to the stability of human lysozyme: Calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants
    • Takano, K., Ogasahara, K., Kaneda, H., Yamagata, Y., Fujii, S., Kanaya, E., Kikuchi, M., Oobatake, M. & Yutani, K. (1995). Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. J. Mol. Biol. 254, 62-76.
    • (1995) J. Mol. Biol. , vol.254 , pp. 62-76
    • Takano, K.1    Ogasahara, K.2    Kaneda, H.3    Yamagata, Y.4    Fujii, S.5    Kanaya, E.6    Kikuchi, M.7    Oobatake, M.8    Yutani, K.9
  • 30
    • 0031050618 scopus 로고    scopus 로고
    • Contribution of the hydrophobic effect to the stability of human lysozyme: Calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants
    • Takano, K., Yamagata, Y., Fujii, S. & Yutani, K. (1997a). Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants. Biochemistry, 36, 688-698.
    • (1997) Biochemistry , vol.36 , pp. 688-698
    • Takano, K.1    Yamagata, Y.2    Fujii, S.3    Yutani, K.4
  • 31
    • 0030696285 scopus 로고    scopus 로고
    • Contribution of water molecules in the interior of a protein to the conformational stability
    • Takano, K., Funahashi, J., Yamagata, Y., Fujii, S. & Yutani, K. (1997b). Contribution of water molecules in the interior of a protein to the conformational stability. J. Mol. Biol. 274, 132-142.
    • (1997) J. Mol. Biol. , vol.274 , pp. 132-142
    • Takano, K.1    Funahashi, J.2    Yamagata, Y.3    Fujii, S.4    Yutani, K.5
  • 32
    • 0023896186 scopus 로고
    • Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae
    • Taniyama, Y., Yamamoto, Y., Nakano, M., Kikuchi, M. & Ikehara, M. (1988). Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 152, 962-967.
    • (1988) Biochem. Biophys. Res. Commun. , vol.152 , pp. 962-967
    • Taniyama, Y.1    Yamamoto, Y.2    Nakano, M.3    Kikuchi, M.4    Ikehara, M.5
  • 33
    • 0026701319 scopus 로고
    • Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast
    • Taniyama, Y., Ogasahara, K., Yutani, K. & Kikuchi, M. (1992). Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast. J. Biol. Chem. 267, 4619-4624.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4619-4624
    • Taniyama, Y.1    Ogasahara, K.2    Yutani, K.3    Kikuchi, M.4
  • 34
    • 0031893269 scopus 로고    scopus 로고
    • The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect
    • Xu, J., Baase, W. A., Baldwin, E. & Matthews, B. W. (1998). The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. Protein Sci. 7, 158-177.
    • (1998) Protein Sci. , vol.7 , pp. 158-177
    • Xu, J.1    Baase, W.A.2    Baldwin, E.3    Matthews, B.W.4
  • 35
    • 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 a subunit
    • 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 a subunit. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.