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Volumn 73, Issue 6, 1997, Pages 3241-3256

Temperature dependence of histidine ionization constants in myoglobin

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE DERIVATIVE; MYOGLOBIN;

EID: 0030865458     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78349-8     Document Type: Article
Times cited : (38)

References (81)
  • 1
    • 0014220273 scopus 로고
    • Reversible denaturation of sperm whale myoglobin. I. Dependence on temperature, pH, and composition
    • Acanipora, G., and J. Hermans. 1967. Reversible denaturation of sperm whale myoglobin. I. Dependence on temperature, pH, and composition. J. Am. Chem. Soc. 89:1543-1552.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 1543-1552
    • Acanipora, G.1    Hermans, J.2
  • 2
    • 0026314673 scopus 로고
    • Electrostatic effects in protein folding, stability, and function
    • Allewell, N. M., and H. Oberoi. 1991. Electrostatic effects in protein folding, stability, and function. Methods Enzymol. 202:3-19.
    • (1991) Methods Enzymol. , vol.202 , pp. 3-19
    • Allewell, N.M.1    Oberoi, H.2
  • 3
    • 84913425878 scopus 로고
    • The dielectric constant of water and Debye-Hückel limiting law slopes
    • Archer, D. G., and P. Wang. 1990. The dielectric constant of water and Debye-Hückel limiting law slopes. J. Phys. Chem. Ref. Data. 19: 371-411.
    • (1990) J. Phys. Chem. Ref. Data , vol.19 , pp. 371-411
    • Archer, D.G.1    Wang, P.2
  • 4
    • 37049089418 scopus 로고
    • Thermodynamics and 1H NMR study of proton complex formation of histidine-containing cyclopeptides in aqueous solution
    • Arena, G., G. Impellizzeri, G. Maccarrone, G. Pappalardo, D. Sciotto, and E. Rizzarelli. 1992. Thermodynamics and 1H NMR study of proton complex formation of histidine-containing cyclopeptides in aqueous solution. J. Chem. Soc. Perkin Trans. 154:371-376.
    • (1992) J. Chem. Soc. Perkin Trans. , vol.154 , pp. 371-376
    • Arena, G.1    Impellizzeri, G.2    Maccarrone, G.3    Pappalardo, G.4    Sciotto, D.5    Rizzarelli, E.6
  • 5
    • 0027245421 scopus 로고
    • Three-state analysis of sperm whale apomyoglobin folding
    • Barrick, D., and R. L. Baldwin. 1993. Three-state analysis of sperm whale apomyoglobin folding. Biochemistry. 32:3790-3796.
    • (1993) Biochemistry , vol.32 , pp. 3790-3796
    • Barrick, D.1    Baldwin, R.L.2
  • 6
    • 0028235775 scopus 로고
    • Molecular mechanisms of acid denaturation: The role of histidine residues in the partial unfolding of apomyoglobin
    • Barrick. D., F. M. Hughson, and R. L. Baldwin. 1994. Molecular mechanisms of acid denaturation: the role of histidine residues in the partial unfolding of apomyoglobin. J. Mol. Biol. 237:588-601.
    • (1994) J. Mol. Biol. , vol.237 , pp. 588-601
    • Barrick, D.1    Hughson, F.M.2    Baldwin, R.L.3
  • 10
    • 0018278632 scopus 로고
    • Proton nuclear magnetic resonance study of histidine ionizations in myoglobins of various species: Comparison of observed and computed pK values
    • Botelho, L. H., S. H. Friend, J. B. Matthew, L. D. Lehman, G. I. H. Hanania, and F. R. N. Gurd. 1978. Proton nuclear magnetic resonance study of histidine ionizations in myoglobins of various species: comparison of observed and computed pK values. Biochemistry. 17:5197-5205.
    • (1978) Biochemistry , vol.17 , pp. 5197-5205
    • Botelho, L.H.1    Friend, S.H.2    Matthew, J.B.3    Lehman, L.D.4    Hanania, G.I.H.5    Gurd, F.R.N.6
  • 11
    • 0000085903 scopus 로고
    • Changes in side chain reactivity accompanying the binding of heme to sperm whale apomyoglobin
    • Breslow, E. 1964. Changes in side chain reactivity accompanying the binding of heme to sperm whale apomyoglobin. J. Biol. Chem. 239: 486-496.
    • (1964) J. Biol. Chem. , vol.239 , pp. 486-496
    • Breslow, E.1
  • 13
    • 0021759017 scopus 로고
    • Assignment of 1H NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy-, and (carbon monoxy)myoglobins
    • Carver, J. A., and J. H. Bradbury. 1984. Assignment of 1H NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy-, and (carbon monoxy)myoglobins. Biochemistry. 23:4890-4905.
    • (1984) Biochemistry , vol.23 , pp. 4890-4905
    • Carver, J.A.1    Bradbury, J.H.2
  • 14
    • 33748476849 scopus 로고
    • Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence
    • Cavanagh, J., and M. Ranee. 1992. Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence. J. Magn. Reson. 96:670-678.
    • (1992) J. Magn. Reson. , vol.96 , pp. 670-678
    • Cavanagh, J.1    Ranee, M.2
  • 15
    • 12044254701 scopus 로고
    • A direct measure of the contribution of solvent reorganization to the enthalpy of ligand binding
    • Chervenak, M. C., and E. J. Toone. 1994. A direct measure of the contribution of solvent reorganization to the enthalpy of ligand binding. J. Am. Chem. Soc. 116:10533-10539.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 10533-10539
    • Chervenak, M.C.1    Toone, E.J.2
  • 16
    • 0020486120 scopus 로고
    • The thermodynamics of myoglobin: Stability effects of axial ligand
    • Cho, K. C., H. T. Poon, and C. L. Choy. 1982. The thermodynamics of myoglobin: stability effects of axial ligand. Biochim. Biophys. Acta. 701:206-215.
    • (1982) Biochim. Biophys. Acta , vol.701 , pp. 206-215
    • Cho, K.C.1    Poon, H.T.2    Choy, C.L.3
  • 17
    • 0026643349 scopus 로고
    • Structural comparison of apomyoglobin and metaquomyoglobin: PH titration of histidines by NMR spectroscopy
    • Cocco, M. J., Y.-H. Kao, A. T. Phillips, and J. T. J. Lecomte. 1992. Structural comparison of apomyoglobin and metaquomyoglobin: pH titration of histidines by NMR spectroscopy. Biochemistry. 31: 6481-6491.
    • (1992) Biochemistry , vol.31 , pp. 6481-6491
    • Cocco, M.J.1    Kao, Y.-H.2    Phillips, A.T.3    Lecomte, J.T.J.4
  • 18
    • 0014664963 scopus 로고
    • Proton magnetic resonance studies of human lysozyme
    • Cohen, J. S. 1969. Proton magnetic resonance studies of human lysozyme. Nature. 223:43-6.
    • (1969) Nature , vol.223 , pp. 43-46
    • Cohen, J.S.1
  • 19
    • 0023660124 scopus 로고
    • 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques
    • 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques. J. Mol. Biol. 194:313-327.
    • (1987) J. Mol. Biol. , vol.194 , pp. 313-327
    • Dalvit, C.1    Wright, P.E.2
  • 20
    • 44949290287 scopus 로고
    • Rapid-pulsing artifacts in double-quantum-filtered COSY
    • Derome, A., and M. Williamson. 1990. Rapid-pulsing artifacts in double-quantum-filtered COSY. J. Magn. Reson. 88:177-185.
    • (1990) J. Magn. Reson. , vol.88 , pp. 177-185
    • Derome, A.1    Williamson, M.2
  • 21
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. 1990. Dominant forces in protein folding. Biochemistry. 29: 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.1
  • 23
    • 0025296867 scopus 로고
    • High-resolution study of the three-dimensional structure of horse heart metmyoglobin
    • Evans, S. V., and G. D. Brayer. 1990. High-resolution study of the three-dimensional structure of horse heart metmyoglobin. J. Mol. Biol. 213:885-897.
    • (1990) J. Mol. Biol. , vol.213 , pp. 885-897
    • Evans, S.V.1    Brayer, G.D.2
  • 24
    • 0000339350 scopus 로고
    • Statistics of the enthalpy-entropy relationship. I-V. The enthalpy entropy relationship in organic reactions
    • Exner, O. 1975. Statistics of the enthalpy-entropy relationship. I-V. The enthalpy entropy relationship in organic reactions. Coll. Czech. Chem. Commun. 40:2762-2791.
    • (1975) Coll. Czech. Chem. Commun. , vol.40 , pp. 2762-2791
    • Exner, O.1
  • 25
    • 0001116663 scopus 로고
    • The ionization of acidic metmyoglobin
    • George, P., and H. Hanania. 1952. The ionization of acidic metmyoglobin. Biochem. J. 52:517-523.
    • (1952) Biochem. J. , vol.52 , pp. 517-523
    • George, P.1    Hanania, H.2
  • 26
    • 0000525863 scopus 로고
    • Solvent reorganization and thermodynamic enthalpy-entropy compensation
    • Grunwald, E., and C. Steel. 1995. Solvent reorganization and thermodynamic enthalpy-entropy compensation. J. Am. Chem. Soc. 117: 5687-5692.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5687-5692
    • Grunwald, E.1    Steel, C.2
  • 27
    • 0019074582 scopus 로고
    • Electrostatic stabilization in sperm whale and harbor seal myoglobins
    • Gurd, F. R. N., S. H. Friend, T. M. Rothgeb, R. S. Gurd, and H. Scouloudi. 1980. Electrostatic stabilization in sperm whale and harbor seal myoglobins. Biophys. J. 10:65-75.
    • (1980) Biophys. J. , vol.10 , pp. 65-75
    • Gurd, F.R.N.1    Friend, S.H.2    Rothgeb, T.M.3    Gurd, R.S.4    Scouloudi, H.5
  • 30
    • 0013787748 scopus 로고
    • Heat of ionization and denaturation of sperm-whale myoglobin determined with a microcalorimeter
    • Hermans, J., Jr., and G. Rialdi. 1965. Heat of ionization and denaturation of sperm-whale myoglobin determined with a microcalorimeter. Biochemistry. 4:1277-1281.
    • (1965) Biochemistry , vol.4 , pp. 1277-1281
    • Hermans J., Jr.1    Rialdi, G.2
  • 31
    • 0015866169 scopus 로고
    • Carbon nuclear magnetic resonance studies of the histidine residue in α-lytic protease: Implications for the catalytic mechanism of serine proteases
    • Hunkapiller, M. W., S. H. Smallcombe, D. R. Whitaker, and J. H. Richards. 1973. Carbon nuclear magnetic resonance studies of the histidine residue in α-lytic protease: implications for the catalytic mechanism of serine proteases. Biochemistry. 12:4732-4743.
    • (1973) Biochemistry , vol.12 , pp. 4732-4743
    • Hunkapiller, M.W.1    Smallcombe, S.H.2    Whitaker, D.R.3    Richards, J.H.4
  • 33
    • 0016203049 scopus 로고
    • Conformation of angiotensin II in aqueous solution: Titration of several peptide analogs and homologs
    • Juliano, L., and A. C. M. Paiva. 1974. Conformation of angiotensin II in aqueous solution: titration of several peptide analogs and homologs. Biochemistry. 13:2445-2450.
    • (1974) Biochemistry , vol.13 , pp. 2445-2450
    • Juliano, L.1    Paiva, A.C.M.2
  • 36
    • 0025290184 scopus 로고
    • A comparative study of the unfolding thermodynamics of vertebrate metmyoglobins
    • Kelly, L., and L. A. Holladay. 1990. A comparative study of the unfolding thermodynamics of vertebrate metmyoglobins. Biochemistry. 29: 5062-5069.
    • (1990) Biochemistry , vol.29 , pp. 5062-5069
    • Kelly, L.1    Holladay, L.A.2
  • 38
    • 0030610243 scopus 로고    scopus 로고
    • a measurements from nuclear magnetic resonance for the B1 and B2 immunogobulin G-binding domains of protein G: Comparison with calculated values for nuclear magnetic resonance and x-ray structures
    • a measurements from nuclear magnetic resonance for the B1 and B2 immunogobulin G-binding domains of protein G: comparison with calculated values for nuclear magnetic resonance and x-ray structures. Biochemistry. 36:3580-3589.
    • (1997) Biochemistry , vol.36 , pp. 3580-3589
    • Khare, D.1    Alexander, P.2    Antosiewicz, J.3    Bryan, P.4    Gilson, M.5    Orban, J.6
  • 39
    • 0343416975 scopus 로고
    • The thermodynamics of ionization of amino acids. II. The ionization constants of some N-acyl amino acids
    • King, E. J., and G. W. King. 1956. The thermodynamics of ionization of amino acids. II. The ionization constants of some N-acyl amino acids. J. Am. Chem. Soc. 78:1089-1099.
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 1089-1099
    • King, E.J.1    King, G.W.2
  • 40
    • 0343852870 scopus 로고
    • Temperature dependence of the structure and dynamics of myoglobin: A simulation approach
    • Kuczera, K., J. Kuryian, and M. Karplus. 1990. Temperature dependence of the structure and dynamics of myoglobin: a simulation approach. J. Mol. Biol. 192:133-154.
    • (1990) J. Mol. Biol. , vol.192 , pp. 133-154
    • Kuczera, K.1    Kuryian, J.2    Karplus, M.3
  • 41
    • 0023042853 scopus 로고
    • X-ray structure and refinement of carbonmonoxy (Fe-II) myoglobin at 1.5 Å resolution
    • Kuriyan, J., S. Wilz, M. Karplus, and G. A. Petsko. 1986. X-ray structure and refinement of carbonmonoxy (Fe-II) myoglobin at 1.5 Å resolution. J. Mol. Biol. 192:133-154.
    • (1986) J. Mol. Biol. , vol.192 , pp. 133-154
    • Kuriyan, J.1    Wilz, S.2    Karplus, M.3    Petsko, G.A.4
  • 42
    • 0030056766 scopus 로고    scopus 로고
    • The native state of apomyoglobin described by proton NMR spectroscopy: The A-B-G-H interface of wild-type sperm whale apomyoglobin
    • Lecomte, J. T. J., Y.-H. Kao, and M. J. Cocco. 1996. The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin. Proteins Struct. Funct. Genet. 25:267-285.
    • (1996) Proteins Struct. Funct. Genet. , vol.25 , pp. 267-285
    • Lecomte, J.T.J.1    Kao, Y.-H.2    Cocco, M.J.3
  • 43
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B., and F. M. Richards. 1971. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 45
    • 0014722597 scopus 로고
    • Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous property of water
    • Lumry, R., and S. Rajender. 1970. Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous property of water. Biopolymers. 9:1125-1227.
    • (1970) Biopolymers , vol.9 , pp. 1125-1227
    • Lumry, R.1    Rajender, S.2
  • 46
    • 0027305948 scopus 로고
    • Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration
    • Makhatadze, G. I., and P. L. Privalov. 1993. Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration. J. Mol. Biol. 232:639-659.
    • (1993) J. Mol. Biol. , vol.232 , pp. 639-659
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 47
    • 0027965116 scopus 로고
    • Hydration effects in protein unfolding
    • Makhatadze, G. I., and P. L. Privalov. 1994. Hydration effects in protein unfolding. Biophys. Chem. 51:291-304.
    • (1994) Biophys. Chem. , vol.51 , pp. 291-304
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 48
    • 0002870406 scopus 로고
    • Observation of histidine residues in proteins by means of nuclear magnetic resonance spectroscopy
    • Markley, J. 1975. Observation of histidine residues in proteins by means of nuclear magnetic resonance spectroscopy. Acc. Chem. Res. 8:70-80.
    • (1975) Acc. Chem. Res. , vol.8 , pp. 70-80
    • Markley, J.1
  • 50
    • 0029967068 scopus 로고    scopus 로고
    • Contributions of the ionizable amino acids to the stability of staphylococcal nuclease
    • Meeker, A. K., B. García-Moreno, and D. Shortle. 1996. Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. Biochemistry. 35:6443-6449.
    • (1996) Biochemistry , vol.35 , pp. 6443-6449
    • Meeker, A.K.1    García-Moreno, B.2    Shortle, D.3
  • 51
    • 0003202948 scopus 로고
    • Non-empirical SCF-MO studies on the protonation of biopolymer constituents. I. Protonation of amino acids
    • Mezey, P. G., J. J. Ladik, and S. Suhai. 1979. Non-empirical SCF-MO studies on the protonation of biopolymer constituents. I. Protonation of amino acids. Theor. Chim. Acta. 51:323-329.
    • (1979) Theor. Chim. Acta , vol.51 , pp. 323-329
    • Mezey, P.G.1    Ladik, J.J.2    Suhai, S.3
  • 52
    • 0002616982 scopus 로고
    • Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence
    • Müller, L. 1979. Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence. J. Am. Chem. Soc. 101: 4481-4484.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 4481-4484
    • Müller, L.1
  • 53
    • 0028232021 scopus 로고
    • Individual ionization constants of all the carboxyl groups in ribonuclease HI from Escherichia coli determined by NMR
    • Oda, Y., T. Yamazaki, K. Nagayama, S. Kanaya, Y. Kuroda, and H. Nakamura. 1994. Individual ionization constants of all the carboxyl groups in ribonuclease HI from Escherichia coli determined by NMR. Biochemistry. 33:5275-5284.
    • (1994) Biochemistry , vol.33 , pp. 5275-5284
    • Oda, Y.1    Yamazaki, T.2    Nagayama, K.3    Kanaya, S.4    Kuroda, Y.5    Nakamura, H.6
  • 54
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., V. Saudek, and V. Sklenar. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 56
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov, P. 1979. Stability of proteins: small globular proteins. Adv. Prot. Chem. 33:167-241.
    • (1979) Adv. Prot. Chem. , vol.33 , pp. 167-241
    • Privalov, P.1
  • 58
    • 0027250627 scopus 로고
    • Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration
    • Privalov, P. L., and O. I. Makhatadze. 1993. Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration. J. Mol. Biol. 232:660-679.
    • (1993) J. Mol. Biol. , vol.232 , pp. 660-679
    • Privalov, P.L.1    Makhatadze, O.I.2
  • 60
    • 0000527952 scopus 로고
    • 1H NMR spectra of proteins using multiple-quantum coherence
    • 1H NMR spectra of proteins using multiple-quantum coherence. J. Magn. Reson. 66: 372-378.
    • (1986) J. Magn. Reson. , vol.66 , pp. 372-378
    • Ranee, M.1    Wright, P.E.2
  • 61
    • 0015934127 scopus 로고
    • Determination of the tautomeric form of the imidazole ring of L-histidine in basic solution by carbon-13 magnetic resonance spectroscopy
    • Reynolds, W. F., I. R. Peat, M. H. Freedman, and J. R. Lyerla. 1973. Determination of the tautomeric form of the imidazole ring of L-histidine in basic solution by carbon-13 magnetic resonance spectroscopy. J. Am. Chem. Soc. 95:328-331.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 328-331
    • Reynolds, W.F.1    Peat, I.R.2    Freedman, M.H.3    Lyerla, J.R.4
  • 62
    • 0014515802 scopus 로고
    • Nuclear magnetic resonance studies of the structure and binding sites of enzymes. VII. Solvent and temperature effects of the ionization of histidine residues of ribonuclease
    • Roberts, G. C. K., D. H. Meadows, and O. Jardetzky. 1969. Nuclear magnetic resonance studies of the structure and binding sites of enzymes. VII. Solvent and temperature effects of the ionization of histidine residues of ribonuclease. Biochemistry. 8:2053-2056.
    • (1969) Biochemistry , vol.8 , pp. 2053-2056
    • Roberts, G.C.K.1    Meadows, D.H.2    Jardetzky, O.3
  • 63
    • 0028951968 scopus 로고
    • pH, ionic strength, and temper ature dependences of ionization equilibria for the carboxyl groups in turkey ovomucoid third domain
    • Schaller, W., and A. D. Robertson. 1995. pH, ionic strength, and temper ature dependences of ionization equilibria for the carboxyl groups in turkey ovomucoid third domain. Biochemistry. 34:4714-23.
    • (1995) Biochemistry , vol.34 , pp. 4714-4723
    • Schaller, W.1    Robertson, A.D.2
  • 64
    • 0016207302 scopus 로고
    • Electrostatic effects in myoglobin: Hydrogen ion equilibria in sperm whale ferrimyoglobin
    • Shire, S. J., G. I. H. Hanania, and F. R. N. Gurd. 1974. Electrostatic effects in myoglobin: hydrogen ion equilibria in sperm whale ferrimyoglobin. Biochemistry. 13:2967-2979.
    • (1974) Biochemistry , vol.13 , pp. 2967-2979
    • Shire, S.J.1    Hanania, G.I.H.2    Gurd, F.R.N.3
  • 66
    • 0024298839 scopus 로고
    • Stability mutants of staphylococcal nuclease: Large compensating enthalpy-entropy changes for the reversible denaturation reaction
    • Shortle, D., A. K. Meeker, and E. Freire. 1988. Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reaction. Biochemistry. 27:4761-4768.
    • (1988) Biochemistry , vol.27 , pp. 4761-4768
    • Shortle, D.1    Meeker, A.K.2    Freire, E.3
  • 67
    • 0015507243 scopus 로고
    • Mathematical model for interacting groups in nuclear magnetic resonance tirration curves
    • Shrager, R. I., J. S. Cohen, S. R. Heller, D. H. Sachs, and A. N. Schlechter. 1972. Mathematical model for interacting groups in nuclear magnetic resonance tirration curves. Biochemistry. 11:541-547.
    • (1972) Biochemistry , vol.11 , pp. 541-547
    • Shrager, R.I.1    Cohen, J.S.2    Heller, S.R.3    Sachs, D.H.4    Schlechter, A.N.5
  • 68
    • 0025191376 scopus 로고
    • Charge effects on folded and unfolded proteins
    • Stigter. D., and K. A. Dill. 1990. Charge effects on folded and unfolded proteins. Biochemistry. 29:1262-1271.
    • (1990) Biochemistry , vol.29 , pp. 1262-1271
    • Stigter, D.1    Dill, K.A.2
  • 69
    • 0000337195 scopus 로고
    • Dependence of NMR lineshape analysis upon chemical rates and mechanisms: Implications for enzyme histidine titrations
    • Sudmeier, J. L., J. L. Evelhoch, and N. B.-H. Jonsson. 1980. Dependence of NMR lineshape analysis upon chemical rates and mechanisms: implications for enzyme histidine titrations. J. Magn. Reson. 40:377-390.
    • (1980) J. Magn. Reson. , vol.40 , pp. 377-390
    • Sudmeier, J.L.1    Evelhoch, J.L.2    Jonsson, N.B.-H.3
  • 70
    • 0017364269 scopus 로고
    • Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of sperm whale metmyoglobin
    • Takano, T. 1977. Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of sperm whale metmyoglobin. J. Mol. Biol. 110:537-568.
    • (1977) J. Mol. Biol. , vol.110 , pp. 537-568
    • Takano, T.1
  • 71
    • 0002014805 scopus 로고
    • Refinement of myoglobin and cytochrome c
    • Oxford University Press, Oxford. U.K.
    • Takano, T. 1984. Refinement of myoglobin and cytochrome c. In Methods and Applications in Crystallographic Computing. Oxford University Press, Oxford. U.K. 262-272.
    • (1984) Methods and Applications in Crystallographic Computing , pp. 262-272
    • Takano, T.1
  • 72
    • 33947461074 scopus 로고
    • Theory of protein titration curves. II. Calculation for simple models at low ionic strength
    • Tanford, C. 1957. Theory of protein titration curves. II. Calculation for simple models at low ionic strength. J. Am. Chem. Soc. 79:5340-5347.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 5340-5347
    • Tanford, C.1
  • 73
    • 33947468892 scopus 로고
    • Theory of protein titration curves. I. General equations for impenetrable spheres
    • Tanford, C., and J. G. Kirkwood. 1957. Theory of protein titration curves. I. General equations for impenetrable spheres. J. Am. Chem. Soc. 79: 5333-5339.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 5333-5339
    • Tanford, C.1    Kirkwood, J.G.2
  • 74
    • 0016818978 scopus 로고
    • Nuclear magnetic resonance titration curves of histidine ring protons: The effect of temperature on ribonuclease
    • Westmoreland, D. G., C. R. Matthews, M. B. Hayes, and J. S. Cohen. 1975. Nuclear magnetic resonance titration curves of histidine ring protons: the effect of temperature on ribonuclease. J. Biol. Chem. 250:7456-7460.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7456-7460
    • Westmoreland, D.G.1    Matthews, C.R.2    Hayes, M.B.3    Cohen, J.S.4
  • 75
    • 0017406976 scopus 로고
    • Titration behavior and tautomeric states of individual histidine residues of myoglobin
    • Wilbur, D. J., and A. Allerhand. 1977. Titration behavior and tautomeric states of individual histidine residues of myoglobin. J. Biol. Chem. 252:4968-4975.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4968-4975
    • Wilbur, D.J.1    Allerhand, A.2
  • 77
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman, J. 1964. Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Prot. Chem. 19:223-286.
    • (1964) Adv. Prot. Chem. , vol.19 , pp. 223-286
    • Wyman, J.1
  • 79
    • 0027231258 scopus 로고
    • On the pH dependence of protein stability
    • Yang, A.-S., and B. Honig. 1993. On the pH dependence of protein stability. J. Mol. Biol. 231:459-474.
    • (1993) J. Mol. Biol. , vol.231 , pp. 459-474
    • Yang, A.-S.1    Honig, B.2
  • 80
    • 0028361968 scopus 로고
    • Structural origins of pH and ionic strength effects on protein stability: Acid denaturation of sperm whale apomyoglobin
    • Yang, A.-S., and B. Honig. 1994. Structural origins of pH and ionic strength effects on protein stability: acid denaturation of sperm whale apomyoglobin. J. Mol. Biol. 237:602-614.
    • (1994) J. Mol. Biol. , vol.237 , pp. 602-614
    • Yang, A.-S.1    Honig, B.2
  • 81
    • 0029986887 scopus 로고    scopus 로고
    • Crystal structures of CO-, deoxy- and met-myoglobins at various pH values
    • Yang, F., and G. N. J. Phillips. 1996. Crystal structures of CO-, deoxy- and met-myoglobins at various pH values. J. Mol. Biol. 256:762-774.
    • (1996) J. Mol. Biol. , vol.256 , pp. 762-774
    • Yang, F.1    Phillips, G.N.J.2


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