메뉴 건너뛰기




Volumn 295, Issue 1, 2000, Pages 127-145

The introduction of strain and its effects on the structure and stability of T4 lysozyme

Author keywords

Cavities; Packing; Protein stability; Structural distortion; Van der Waals interaction

Indexed keywords

ALANINE; ISOLEUCINE; LEUCINE; LYSOZYME; METHIONINE; MUTANT PROTEIN; PHENYLALANINE; TRYPTAMINE; VALINE;

EID: 0034614649     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3300     Document Type: Article
Times cited : (52)

References (37)
  • 1
    • 0023494191 scopus 로고
    • Structural and thermal stability of phage T4 lysozyme
    • Alber T., Matthews B. W. Structural and thermal stability of phage T4 lysozyme. Methods Enzymol. 154:1987;511-533.
    • (1987) Methods Enzymol. , vol.154 , pp. 511-533
    • Alber, T.1    Matthews, B.W.2
  • 2
    • 0027209738 scopus 로고
    • Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser117→Phe
    • Anderson D. E., Hurley J. H., Nicholson H., Baase W. A., Matthews B. W. Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser117→Phe. Protein Sci. 2:1993;1285-1290.
    • (1993) Protein Sci. , vol.2 , pp. 1285-1290
    • Anderson, D.E.1    Hurley, J.H.2    Nicholson, H.3    Baase, W.A.4    Matthews, B.W.5
  • 3
    • 0027716138 scopus 로고
    • The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme
    • Baldwin E. P., Hajiseyedjavadi O., Baase W. A., Matthews B. W. The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. Science. 262:1993;1715-1718.
    • (1993) Science , vol.262 , pp. 1715-1718
    • Baldwin, E.P.1    Hajiseyedjavadi, O.2    Baase, W.A.3    Matthews, B.W.4
  • 4
    • 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 B. W. Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. J. Mol. Biol. 259:1996;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
  • 5
    • 0023334744 scopus 로고
    • Thermal denaturation of bacteriophage T4 lysozyme at neutral pH
    • Becktel W. J., Baase W. A. Thermal denaturation of bacteriophage T4 lysozyme at neutral pH. Biopolymers. 26:1987;619-623.
    • (1987) Biopolymers , vol.26 , pp. 619-623
    • Becktel, W.J.1    Baase, W.A.2
  • 6
    • 0027485997 scopus 로고
    • Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala→Ser and Val→Thr substitutions in T4 lysozyme
    • Blaber M., Lindstrom J. D., Gassner N., Xu J., Heinz D. W., Matthews B. W. Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala→Ser and Val→Thr substitutions in T4 lysozyme. Biochemistry. 32:1993;11363-11373.
    • (1993) Biochemistry , vol.32 , pp. 11363-11373
    • Blaber, M.1    Lindstrom, J.D.2    Gassner, N.3    Xu, J.4    Heinz, D.W.5    Matthews, B.W.6
  • 7
    • 0028178528 scopus 로고
    • Determination of α-helix propensity within the context of a folded protein: Sites 44 and 131 in bacteriophage T4 lysozyme
    • Blaber M., Zhang X-J., Lindstrom J. D., Pepiot S. D., Baase W. A., Matthews B. W. Determination of α-helix propensity within the context of a folded protein: sites 44 and 131 in bacteriophage T4 lysozyme. J. Mol. Biol. 235:1994;600-624.
    • (1994) J. Mol. Biol. , vol.235 , pp. 600-624
    • Blaber, M.1    Zhang, X.-J.2    Lindstrom, J.D.3    Pepiot, S.D.4    Baase, W.A.5    Matthews, B.W.6
  • 8
    • 0026665778 scopus 로고
    • Side-chain entropy opposes α-helix formation but rationalizes experimentally determined helix-forming propensities
    • Creamer T. P., Rose G. D. Side-chain entropy opposes α-helix formation but rationalizes experimentally determined helix-forming propensities. Proc. Natl Acad. Sci. USA. 89:1992;5937-5941.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5937-5941
    • Creamer, T.P.1    Rose, G.D.2
  • 9
    • 0025321279 scopus 로고
    • A mutant T4 lysozyme (Val131→Ala) designed to increase thermostability by reduction of strain within an α-helix
    • Dao-pin S., Baase W. A., Matthews B. W. A mutant T4 lysozyme (Val131→Ala) designed to increase thermostability by reduction of strain within an α-helix. Proteins: Struct. Funct. Genet. 7:1990;198-204.
    • (1990) Proteins: Struct. Funct. Genet. , vol.7 , pp. 198-204
    • Dao-Pin, S.1    Baase, W.A.2    Matthews, B.W.3
  • 10
    • 0025822990 scopus 로고
    • Structural and thermodynamic analysis of the packing of two α-helices in bacteriophage T4 lysozyme
    • Dao-pin S., Albert T., Baase W. A., Wozniak J. A., Matthews B. W. Structural and thermodynamic analysis of the packing of two α-helices in bacteriophage T4 lysozyme. J. Mol. Biol. 221:1991;647-667.
    • (1991) J. Mol. Biol. , vol.221 , pp. 647-667
    • Dao-Pin, S.1    Albert, T.2    Baase, W.A.3    Wozniak, J.A.4    Matthews, B.W.5
  • 11
    • 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 A. E., Baase W. A., Matthews B. W. Similar hydrophobic replacements of Leu 99 and Phe 153 within the core of T4 lysozyme have different structural and thermodynamic consequences. J. Mol. Biol. 229:1993;747-769.
    • (1993) J. Mol. Biol. , vol.229 , pp. 747-769
    • Eriksson, A.E.1    Baase, W.A.2    Matthews, B.W.3
  • 12
    • 0000484499 scopus 로고
    • Hydrophobic parameters p of amino acid side-chains form the partioning of N-acetyl-amino-acid amides
    • Fauchere J.-L., Pliska V. Hydrophobic parameters p of amino acid side-chains form the partioning of N-acetyl-amino-acid amides. Eur. J. Med. Chem. 18:1983;369-375.
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchere, J.-L.1    Pliska, V.2
  • 14
    • 0022293584 scopus 로고
    • Multiwire area X-ray diffractometers
    • Hamlin R. Multiwire area X-ray diffractometers. Methods Enzymol. 114:1985;416-452.
    • (1985) Methods Enzymol. , vol.114 , pp. 416-452
    • Hamlin, R.1
  • 15
    • 0026532266 scopus 로고
    • Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme
    • Hurley J. H., Baase W. A., Matthews B. W. Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. J. Mol. Biol. 224:1992;1143-1159.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1143-1159
    • Hurley, J.H.1    Baase, W.A.2    Matthews, B.W.3
  • 17
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 18
    • 0028147533 scopus 로고
    • Crystal structure of a mutant protein with altered but improved hydrophobic core packing
    • Lim W. A., Hodel A., Sauer R. T., Richards F. M. Crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proc. Natl Acad. Sci. USA. 91:1994;423-427.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 423-427
    • Lim, W.A.1    Hodel, A.2    Sauer, R.T.3    Richards, F.M.4
  • 20
    • 0024564552 scopus 로고
    • Control of enzyme activity by an engineered disulfide bond
    • Matsumura M., Matthews B. W. Control of enzyme activity by an engineered disulfide bond. Science. 243:1989;792-794.
    • (1989) Science , vol.243 , pp. 792-794
    • Matsumura, M.1    Matthews, B.W.2
  • 21
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 22
    • 0029411262 scopus 로고
    • Occluded molecular surface analysis of protein packing
    • Pattabiraman N., Ward K. B., Fleming P. J. Occluded molecular surface analysis of protein packing. J. Mol. Recogn. 8:1995;334-344.
    • (1995) J. Mol. Recogn. , vol.8 , pp. 334-344
    • Pattabiraman, N.1    Ward, K.B.2    Fleming, P.J.3
  • 23
    • 0027367252 scopus 로고
    • Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by hydrogen bonding via bound solvent
    • Pjura P., Matthews B. W. Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by hydrogen bonding via bound solvent. Protein Sci. 2:1993;2226-2232.
    • (1993) Protein Sci. , vol.2 , pp. 2226-2232
    • Pjura, P.1    Matthews, B.W.2
  • 24
    • 0025761294 scopus 로고
    • Second-site revertants of an inactive T4 lysozyme mutant restore activity structuring the active site cleft
    • Poteete A. R., Dao-pin S., Nicholson H., Matthews B. W. Second-site revertants of an inactive T4 lysozyme mutant restore activity structuring the active site cleft. Biochemistry. 30:1991;1425-1432.
    • (1991) Biochemistry , vol.30 , pp. 1425-1432
    • Poteete, A.R.1    Dao-Pin, S.2    Nicholson, H.3    Matthews, B.W.4
  • 25
    • 0015977588 scopus 로고
    • The interpretation of protein structures: Total volume, group volume distributions and packing density
    • Richards F. M. The interpretation of protein structures: Total volume, group volume distributions and packing density. J. Mol. Biol. 82:1974;1-14.
    • (1974) J. Mol. Biol. , vol.82 , pp. 1-14
    • Richards, F.M.1
  • 26
    • 0027815614 scopus 로고
    • An analysis of packing in the protein folding problem
    • Richards F. M., Lim W. A. An analysis of packing in the protein folding problem. Quart. Rev. Biophys. 26:1994;423-498.
    • (1994) Quart. Rev. Biophys. , vol.26 , pp. 423-498
    • Richards, F.M.1    Lim, W.A.2
  • 27
    • 0024400292 scopus 로고
    • Influence of interior packing and hydrophobicity on the stability of a protein
    • Sandberg W. S., Terwilliger T. C. Influence of interior packing and hydrophobicity on the stability of a protein. Science. 245:1989;54-57.
    • (1989) Science , vol.245 , pp. 54-57
    • Sandberg, W.S.1    Terwilliger, T.C.2
  • 28
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud D. E., Ten Eyck L. F., Matthews B. W. An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallog. sect. A. 43:1987;489-503.
    • (1987) Acta Crystallog. Sect. a , vol.43 , pp. 489-503
    • Tronrud, D.E.1    Ten, E.L.F.2    Matthews, B.W.3
  • 29
    • 0026998178 scopus 로고
    • Crystallographic structures of ribonuclease S variants with nonpolar substitution at position 13: Packing and cavities
    • Varadarajan R., Richards F. M. Crystallographic structures of ribonuclease S variants with nonpolar substitution at position 13: packing and cavities. Biochemistry. 31:1992;12315-12327.
    • (1992) Biochemistry , vol.31 , pp. 12315-12327
    • Varadarajan, R.1    Richards, F.M.2
  • 30
    • 0030462974 scopus 로고    scopus 로고
    • Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme
    • Vetter I. R., Baase W. A., Heinz D. W., Xiong J.-P., Snow S., Matthews B. W. Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme. Protein Sci. 5:1996;2399-2415.
    • (1996) Protein Sci. , vol.5 , pp. 2399-2415
    • Vetter, I.R.1    Baase, W.A.2    Heinz, D.W.3    Xiong, J.-P.4    Snow, S.5    Matthews, B.W.6
  • 31
    • 0023104358 scopus 로고
    • Structure of bacteriophage T4 lysozyme refined at 1.7 Å resolution
    • Weaver L. H., Matthews B. W. Structure of bacteriophage T4 lysozyme refined at 1.7 Å resolution. J. Mol. Biol. 193:1987;189-199.
    • (1987) J. Mol. Biol. , vol.193 , pp. 189-199
    • Weaver, L.H.1    Matthews, B.W.2
  • 32
    • 0029977512 scopus 로고    scopus 로고
    • Mobile unnatural amino acid side-chains in the core of the staphylococcal nuclease
    • Wynn R., Harkins P. C., Richards F. M., Fox R. O. Mobile unnatural amino acid side-chains in the core of the staphylococcal nuclease. Protein Sci. 5:1996;1026-1031.
    • (1996) Protein Sci. , vol.5 , pp. 1026-1031
    • Wynn, R.1    Harkins, P.C.2    Richards, F.M.3    Fox, R.O.4
  • 33
    • 0030762019 scopus 로고    scopus 로고
    • Comparison of straight chain and cyclic unnatural amino acids embedded in the core of staphylococcal nuclease
    • Wynn R., Harkins P. C., Richards F. M., Fox R. O. Comparison of straight chain and cyclic unnatural amino acids embedded in the core of staphylococcal nuclease. Protein Sci. 6:1997;1621-1626.
    • (1997) Protein Sci. , vol.6 , pp. 1621-1626
    • Wynn, R.1    Harkins, P.C.2    Richards, F.M.3    Fox, R.O.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. The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. Protein Sci. 7:1998;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
    • 0027606637 scopus 로고
    • STRAT: A program to optimize X-ray data collection on an area detector system
    • Zhang X.-J., Matthews B. W. STRAT: a program to optimize X-ray data collection on an area detector system. J. Appl. Crystallog. 26:1993;457-462.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 457-462
    • Zhang, X.-J.1    Matthews, B.W.2
  • 36
    • 0028878767 scopus 로고
    • EDPDB: A multi-functional tool for protein structure analysis
    • Zhang X.-J., Matthews B. W. EDPDB: a multi-functional tool for protein structure analysis. J. Appl. Crystallog. 28:1995;624-630.
    • (1995) J. Appl. Crystallog. , vol.28 , pp. 624-630
    • Zhang, X.-J.1    Matthews, B.W.2
  • 37
    • 0029150760 scopus 로고
    • Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme
    • Zhang X.-J., Wozniak J. A., Matthews B. W. Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. J. Mol. Biol. 250:1995;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.