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Volumn 7, Issue 1, 1998, Pages 158-177

The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect

Author keywords

Alanine; Cavities; Core packing; Hydrophobic effect; T4 lysozyme

Indexed keywords

LYSOZYME;

EID: 0031893269     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070117     Document Type: Article
Times cited : (219)

References (43)
  • 1
    • 0023668221 scopus 로고
    • Temperature-sensitive mutations of baeteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein
    • Alber T, Dao-pin S, Nye JA, Muchmore DC, Matthews BW. 1987. Temperature-sensitive mutations of baeteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein. Biochemistry 26:3754-3758.
    • (1987) Biochemistry , vol.26 , pp. 3754-3758
    • Alber, T.1    Dao-pin, S.2    Nye, J.A.3    Muchmore, D.C.4    Matthews, B.W.5
  • 2
    • 0029892667 scopus 로고    scopus 로고
    • Thermodynamic and structural compensation in "size-switch" core repacking variants of T4 lysozyme
    • Baldwin E, Xu J, Hajiseyedjavadi O, Baase WA, Matthews BW. 1996. Thermodynamic and structural compensation in "size-switch" core repacking variants of 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, B.W.5
  • 4
    • 0025909418 scopus 로고
    • Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium and high ionic strengths
    • Bell JA, Wilson KP, Zhang X-J, Faber HR, Nicholson H, Matthews BW. 1991. Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium and high ionic strengths. Proteins 10:10-21.
    • (1991) Proteins , vol.10 , pp. 10-21
    • Bell, J.A.1    Wilson, K.P.2    Zhang, X.-J.3    Faber, H.R.4    Nicholson, H.5    Matthews, B.W.6
  • 5
    • 0011429211 scopus 로고
    • Structure of proteins
    • Bernal JD. 1939. Structure of proteins. Nature 143:663-667.
    • (1939) Nature , vol.143 , pp. 663-667
    • Bernal, J.D.1
  • 6
    • 0028920304 scopus 로고
    • Alanine scanning mutagenesis of the α-helix 115-123 of phage T4 lysozyme: Effects on structure, stability and the binding of solvent
    • Blaber M, Baase WA, Gassner N, Matthews BW. 1995. Alanine scanning mutagenesis of the α-helix 115-123 of phage T4 lysozyme: Effects on structure, stability and the binding of solvent. J Mol Biol 246:317-330.
    • (1995) J Mol Biol , vol.246 , pp. 317-330
    • Blaber, M.1    Baase, W.A.2    Gassner, N.3    Matthews, B.W.4
  • 7
    • 0014201797 scopus 로고
    • The thermodynamics of protein denaturation. III. the denaturation of ribonuclease in water and in aqueous urea and aqueous ethanol mixtures
    • Brandts JF, Hunt L. 1967. The thermodynamics of protein denaturation. III. The denaturation of ribonuclease in water and in aqueous urea and aqueous ethanol mixtures. J Am Chem Soc 89:4826-4838.
    • (1967) J Am Chem Soc , vol.89 , pp. 4826-4838
    • Brandts, J.F.1    Hunt, L.2
  • 8
    • 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 AM, Cramer P, Fersht AR. 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
  • 9
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly ML. 1983. Solvent-accessible surfaces of proteins and nucleic acids. Science 221:709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 10
    • 0023645034 scopus 로고
    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • Cornette JL, Cease KB, Margalit H, Spouge JL, Berzofsky JA, DeLisi C. 1987. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J Mol Biol 195:659-685.
    • (1987) J Mol Biol , vol.195 , pp. 659-685
    • Cornette, J.L.1    Cease, K.B.2    Margalit, H.3    Spouge, J.L.4    Berzofsky, J.A.5    Delisi, C.6
  • 11
    • 0025321279 scopus 로고
    • A mutant T4 lysozyme (Val 131 Ala) designed to increase thermostability by the reduction of strain within an α-helix
    • Dao-pin S, Baase WA, Matthews BW. 1990. A mutant T4 lysozyme (Val 131 Ala) designed to increase thermostability by the reduction of strain within an α-helix. Proteins 7:198-204.
    • (1990) Proteins , vol.7 , pp. 198-204
    • Dao-pin, S.1    Baase, W.A.2    Matthews, B.W.3
  • 12
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. 1990. Dominant forces in protein folding. Biochemistry 29:7133-74155.
    • (1990) Biochemistry , vol.29 , pp. 7133-74155
    • Dill, K.A.1
  • 13
    • 0026567907 scopus 로고
    • The response of a protein structure to cavity-creating mutations and its relationship to the hydrophobic effect
    • Eriksson AE, Baase WA, Zhang X-J, Heinz DW, Blaber M, Baldwin EP, Matthews BW. 1992. The response of a protein structure to cavity-creating mutations and its relationship 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
  • 14
    • 0027394606 scopus 로고
    • Similar hydrophobic replacements of Leu 99 and Phe 153 within the core of T4 lysozyme have different structural and thermodynamic consequences
    • Eriksson AE, Baase WA, Matthews BW. 1993. Similar hydrophobic replacements of Leu 99 and Phe 153 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
  • 15
    • 0025047629 scopus 로고
    • A mutant T4 lysozyme displays five different crystal conformations
    • Faber HR, Matthews BW. 1990. A mutant T4 lysozyme displays five different crystal conformations. Nature 348:263-266.
    • (1990) Nature , vol.348 , pp. 263-266
    • Faber, H.R.1    Matthews, B.W.2
  • 16
    • 0000484499 scopus 로고
    • Hydrophobic parameters π of amino acid sidechains form the partitioning of N-acetyl-amino-acid amides
    • Fauchére J-L, Pliška V. 1983. Hydrophobic parameters π of amino acid sidechains form the partitioning of N-acetyl-amino-acid amides. Eur J Med Chem 18:369-375.
    • (1983) Eur J Med Chem , vol.18 , pp. 369-375
    • Fauchére, J.-L.1    Pliška, V.2
  • 17
    • 0022293584 scopus 로고
    • Multiwire area X-ray diffractometers
    • Hamlin R. 1985. Multiwire area X-ray diffractometers. Meth Enzymol 114:416-452.
    • (1985) Meth Enzymol , vol.114 , pp. 416-452
    • Hamlin, R.1
  • 18
    • 0028354690 scopus 로고
    • Accommodation of amino acid insertions in an α-helix of T4 lysozyme. Structural and thermodynamic analysis
    • Heinz DW, Baase WA, Zhang X-J, Blaber M, Dahlquist FW, Matthews BW. 1994. Accommodation of amino acid insertions in an α-helix of T4 lysozyme. Structural and thermodynamic analysis. J Mol Biol 236:869-886.
    • (1994) J Mol Biol , vol.236 , pp. 869-886
    • Heinz, D.W.1    Baase, W.A.2    Zhang, X.-J.3    Blaber, M.4    Dahlquist, F.W.5    Matthews, B.W.6
  • 20
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. 1959. Some factors in the interpretation of protein denaturation. Adv Protein Chem 16:1-63.
    • (1959) Adv Protein Chem , vol.16 , pp. 1-63
    • Kauzmann, W.1
  • 21
    • 0024375463 scopus 로고
    • Energetics of complementary sidechain packing in a protein hydrophohic core
    • Kellis JT Jr, Nyberg K, Fersht AR. 1989. Energetics of complementary sidechain packing in a protein hydrophohic core. Biochemistry 28:4914-4922.
    • (1989) Biochemistry , vol.28 , pp. 4914-4922
    • Kellis Jr., J.T.1    Nyberg, K.2    Fersht, A.R.3
  • 22
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt GJ, Jones TA. 1994. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Cryst D50:178-185.
    • (1994) Acta Cryst , vol.D50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 23
    • 0023741058 scopus 로고
    • Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3
    • Matsumura M, Becktel WJ, Matthews BW. 1988. Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature 334:406-410.
    • (1988) Nature , vol.334 , pp. 406-410
    • Matsumura, M.1    Becktel, W.J.2    Matthews, B.W.3
  • 24
    • 0024564552 scopus 로고
    • Control of enzyme activity by an engineered disulfide bond
    • Matsumura M, Matthews BW. 1989. Control of enzyme activity by an engineered disulfide bond. Science 243:792-794.
    • (1989) Science , vol.243 , pp. 792-794
    • Matsumura, M.1    Matthews, B.W.2
  • 25
    • 0024450809 scopus 로고
    • Structural studies of mutants of T4 lysozyme that alter hydrophobic stabilization
    • Matsumura M, Wozniak JA, Dao-pin S, Matthews BW. 1989. Structural studies of mutants of T4 lysozyme that alter hydrophobic stabilization. J Biol Chem 264:16059-16066.
    • (1989) J Biol Chem , vol.264 , pp. 16059-16066
    • Matsumura, M.1    Wozniak, J.A.2    Dao-pin, S.3    Matthews, B.W.4
  • 26
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews BW. 1993. Structural and genetic analysis of protein stability. Ann Rev Biochem 62:139-160.
    • (1993) Ann Rev Biochem , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 27
    • 0029067489 scopus 로고
    • Specificity of ligand binding in a buried non-polar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity
    • Morton A, Matthews BW. 1995. Specificity of ligand binding in a buried non-polar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity. Biochemistry 34:8576-8588.
    • (1995) Biochemistry , vol.34 , pp. 8576-8588
    • Morton, A.1    Matthews, B.W.2
  • 28
    • 0000181415 scopus 로고
    • The influence of amino acid sidechains on the free energy of helix-coil transitions
    • Nemethy G, Leach SJ, Scheraga HA. 1966. The influence of amino acid sidechains on the free energy of helix-coil transitions. J Phys Chem 70:998-1004.
    • (1966) J Phys Chem , vol.70 , pp. 998-1004
    • Nemethy, G.1    Leach, S.J.2    Scheraga, H.A.3
  • 29
    • 0026010011 scopus 로고
    • Analysis of the interaction between charged sidechains and the a-helix dipole using designed thermostable mutants of phage T4 lysozyme
    • Nicholson H, Anderson DE, Dao-pin S, Matthews BW. 1991. Analysis of the interaction between charged sidechains and the a-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry 30:9816-9828.
    • (1991) Biochemistry , vol.30 , pp. 9816-9828
    • Nicholson, H.1    Anderson, D.E.2    Dao-pin, S.3    Matthews, B.W.4
  • 30
    • 0028865428 scopus 로고
    • Structural factors contributing to the hydrophobic effect: The partly exposed hydrophobic minicore in chymotrypsin inhibitor 2
    • Otzen DE, Rheinnecker M, Fersht AR. 1995. Structural factors contributing to the hydrophobic effect: The partly exposed hydrophobic minicore in chymotrypsin inhibitor 2. Biochemistry 34:13051-13058.
    • (1995) Biochemistry , vol.34 , pp. 13051-13058
    • Otzen, D.E.1    Rheinnecker, M.2    Fersht, A.R.3
  • 31
    • 0025761294 scopus 로고
    • Second-site revertants of an inactive T4 lysozyme mutant restore activity structuring the active site cleft
    • Poteete AR, Dao-pin S, Nicholson H., Matthews BW. 1991. Second-site revertants of an inactive T4 lysozyme mutant restore activity structuring the active site cleft. Biochemistry 30:1425-1432.
    • (1991) Biochemistry , vol.30 , pp. 1425-1432
    • Poteete, A.R.1    Dao-pin, S.2    Nicholson, H.3    Matthews, B.W.4
  • 32
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards FM. 1977. Areas, volumes, packing and protein structure. Ann Rev Biophys Bioeng 6:151-176.
    • (1977) Ann Rev Biophys Bioeng , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 33
    • 0027815614 scopus 로고
    • An analysis of packing in the protein folding problem
    • Richards FM, Lim WA. 1994. An analysis of packing in the protein folding problem. Quart Rev Biophys 26:423-498.
    • (1994) Quart Rev Biophys , vol.26 , pp. 423-498
    • Richards, F.M.1    Lim, W.A.2
  • 35
    • 0026416668 scopus 로고
    • Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects
    • Sharp KA, Nicholls A, Fine RF, Honig B. 1991. Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects. Science 252:106-109.
    • (1991) Science , vol.252 , pp. 106-109
    • Sharp, K.A.1    Nicholls, A.2    Fine, R.F.3    Honig, B.4
  • 36
    • 0025005525 scopus 로고
    • Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease
    • Shortle D, Stites WE, Meeker AK. 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
  • 37
    • 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
  • 38
    • 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. 1997. 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
  • 39
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud DE, Ten Eyck LF, Matthews BW. 1987. An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Cryst A43:489-503.
    • (1987) Acta Cryst , vol.A43 , pp. 489-503
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 40
    • 0026998178 scopus 로고
    • Crystallographic structures of ribonuclease S variants with nonpolar substitution at position 13: Packing and cavities
    • Varadarajan R, Richards FM. 1992. Crystallographic structures of ribonuclease S variants with nonpolar substitution at position 13: Packing and cavities. Biochemistry 31:12315-12327.
    • (1992) Biochemistry , vol.31 , pp. 12315-12327
    • Varadarajan, R.1    Richards, F.M.2
  • 41
    • 0023368698 scopus 로고
    • Dependence of conformation stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase α-subunit
    • Yutani K, Ogasahara K, Tsujita T, Sugino Y. 1987. Dependence of conformation stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase α-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
  • 42
    • 0027606637 scopus 로고
    • STRAT: A program to optimize X-ray data collection on an area detector system
    • Zhang X-J, Matthews BW. 1993. STRAT: A program to optimize X-ray data collection on an area detector system. J Appl Cryst 26:457-462.
    • (1993) J Appl Cryst , vol.26 , pp. 457-462
    • Zhang, X.-J.1    Matthews, B.W.2
  • 43
    • 0029150760 scopus 로고
    • Protein flexibility and adaptability seen in 25 crystals forms of T4 lysozyme
    • Zhang X-J, Wozniak JA, Matthews BW. 1995. Protein flexibility and adaptability seen in 25 crystals forms of T4 lysozyme. J Mol Biol 250:527-552.
    • (1995) J Mol Biol , vol.250 , pp. 527-552
    • Zhang, X.-J.1    Wozniak, J.A.2    Matthews, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.