SEARCH

SEARCH BY CITATION

References

  • 1
    Grütter MG, Hawkes RB, Matthews BW ( 1979) Molecular basis of thermostability in the lysozyme from bacteriophage T4. Nature 277: 667669.
  • 2
    Hawkes R, Grütter MG, Schellman J ( 1984) Thermodynamic stability and point mutations of bacteriophage T4 lysozyme. J Mol Biol 175: 195212.
  • 3
    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: 37883792.
  • 4
    Weaver LH, Gray TM, Grütter MG, Anderson DE, Wozniak JA, Dahlquist FW, Matthews BW ( 1989) High-resolution structure of the temperature-sensitive mutant of phage lysozyme. Arg96 → His Biochemistry 28: 37933797.
  • 5
    Tidor B, Karplus M ( 1991) Simulation analysis of the stability mutant R96H of T4 lysozyme. Biochemistry 30: 32173228.
  • 6
    Mattos C, Cohen JD, Greene DF, Tidor B, Karplus M ( 2004) X-ray structural and simulation analysis of a protein mutant: the value of a combined approach. Proteins 55: 733742.
  • 7
    Mooers BHM, Tronrud DE, Matthews BW. Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg96 → His. Protein Sci 18: 863870.
  • 8
    Mooers BHM, Matthews BW ( 2004) Use of an ion binding site to bypass the 1000-atom limit to structure determination by direct methods. Acta Cryst D 60: 17261737.
  • 9
    Creighton TE ( 1992) Proteins: structures and molecular properties, 2nd ed. New York: W.H. Freeman and Company, p 6.
  • 10
    Blaber M, Lindstrom JD, Gassner N, Xu J, Heinz DW, Matthews BW ( 1993) 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: 1136311373.
  • 11
    Blaber M, Zhang X-J, Lindstrom JD, Pepiot SD, Baase WA, Matthews BW ( 1994) Determination of α-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J Mol Biol 235: 600624.
  • 12
    Pace CN, Alston RW, Shaw KL ( 2000) Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Protein Sci 9: 13951398.
  • 13
    Takano K, Scholtz JM, Sacchettini JC, Pace CN ( 2003) The contribution of polar group burial to protein stability is strongly context-dependent. J Biol Chem 278: 3179031795.
  • 14
    Doig AJ, Sternberg MJE ( 1995) Side-chain conformational entropy in protein folding. Protein Sci 4: 22472251.
  • 15
    Kunkel TA ( 1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 82: 488492.
  • 16
    Landt O, Grunert H-P, Hahn U ( 1990) A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene 96: 125128.
  • 17
    Alber T, Dao-pin S, Nye JA, Muchmore DC, Matthews BW ( 1987) Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein. Biochemistry 26: 37543758.
  • 18
    Muchmore DC, McIntosh LP, Russell CB, Anderson DE, Dahlquist FW ( 1989) Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol 177: 4473.
  • 19
    Poteete AR, Sun D-P, Nicholson H, Matthews BW ( 1991) Second-site revertants of an inactive T4 lysozyme mutant restore activity restructuring the active site cleft. Biochemistry 30: 14251432.
  • 20
    Eriksson AE, Baase WA, Matthews BW ( 1993) Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. J Mol Biol 229: 747769.
  • 21
    Elwell M, Schellman JA ( 1975) Phage T4 lysozyme. Physical properties and reversible unfolding. Biochim Biophys Acta 386: 309323.
  • 22
    Zhang X-J, Baase WA, Shoichet BK, Wilson KP, Matthews BW ( 1995) Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. Protein Eng 8: 10171022.
  • 23
    Lipscomb LA, Gassner NC, Snow SD, Eldridge AM, Baase WA, Drew DL, Matthews BW ( 1998) Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme. Protein Sci 7: 765773.
  • 24
    Hamlin R ( 1985) Multiwire area X-ray diffractometers. Methods Enzymol 114: 416452.
  • 25
    Otwinowski Z, Minor W ( 1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307326.
  • 26
    Kabsch W ( 1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26: 795800.
  • 27
    Kissinger CR, Gehlhaar DK, Fogel DB ( 1999) Rapid automated molecular replacement by evolutionary search. Acta Cryst D 55: 484491.
  • 28
    Vagin A, Teplyakov A ( 1997) MOLREP: an automated program for molecular replacement. J Appl Cryst 30: 10221025.
  • 29
    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: 1021.
  • 30
    Tronrud DE, Ten Eyck LF, Matthews BW ( 1987) An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Cryst A 43: 489501.
  • 31
    Tronrud DE ( 1997) TNT refinement package. Methods Enzymol 277: 306319.
  • 32
    Murshudov GN, Vagin AA, Dodson EJ ( 1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst D 53: 240255.
  • 33
    Murshudov GN, Vagin AA, Lebedev A, Wilson KS, Dodson EJ ( 1999) Efficient anisotropic refinement of macromolecular structures using FFT. Acta Cryst D 55: 247255.
  • 34
    Adams PD, Grosse-Kunstleve RW, Hung L-W, Iorger TR, McCoy AJ, Moriarty NW, Read RJ, Sacchettini JC, Sauter NK, Terwilliger TC ( 2002) PHENIX: building new software for automated crystallographic structure determination. Acta Cryst D 58: 19481954.
  • 35
    McRee DE ( 1999) XtalView/Xfit—a versatile program for manipulating atomic coordinates and electron density. J Struct Biol 125: 156165.
  • 36
    Kraulis PJ ( 1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24: 946950.