-
1
-
-
0014220273
-
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
-
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
-
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
-
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
-
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
-
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
-
8
-
-
0030835046
-
The tautomeric state of histidines in myoglobin
-
Bhattacharya, S., S. F. Sukits, K. L. MacLaughlin, and J. T. J. Lecomte. 1997. The tautomeric state of histidines in myoglobin. Biophys. J. 73:3230-3240.
-
(1997)
Biophys. J.
, vol.73
, pp. 3230-3240
-
-
Bhattacharya, S.1
Sukits, S.F.2
MacLaughlin, K.L.3
Lecomte, J.T.J.4
-
9
-
-
0002960348
-
Ionization constants and thermodynamic parameters of histidine and derivatives
-
Boschcov, P. W., W. S. Seodel, J. Muradian, M. Tominaga, A. C. M. Paiva, and L. Juliano. 1983. Ionization constants and thermodynamic parameters of histidine and derivatives. Bioorg. Chem. 12:34-44.
-
(1983)
Bioorg. Chem.
, vol.12
, pp. 34-44
-
-
Boschcov, P.W.1
Seodel, W.S.2
Muradian, J.3
Tominaga, M.4
Paiva, A.C.M.5
Juliano, L.6
-
10
-
-
0018278632
-
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
-
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
-
12
-
-
0014422643
-
The transition between 'acid' and 'alkaline' ferric heme proteins
-
Brunori, M., G. Amiconi, E. Antonini, J. Wyman, R. Zito, and R. Fanelli. 1968. The transition between 'acid' and 'alkaline' ferric heme proteins. Biochim. Biophys. Acta. 154:315-322.
-
(1968)
Biochim. Biophys. Acta
, vol.154
, pp. 315-322
-
-
Brunori, M.1
Amiconi, G.2
Antonini, E.3
Wyman, J.4
Zito, R.5
Fanelli, R.6
-
13
-
-
0021759017
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
28
-
-
0020170342
-
Conformational substates in a protein: Structure and dynamics of metmyoglobin at 80 K
-
Hartmann, H., F. Parak, W. Steigemann, G. A. Petsko, and D. R. Ponzi. 1982. Conformational substates in a protein: structure and dynamics of metmyoglobin at 80 K. Proc. Natl. Acad. Sci. U.S.A. 79:4967-4971.
-
(1982)
Proc. Natl. Acad. Sci. U.S.A.
, vol.79
, pp. 4967-4971
-
-
Hartmann, H.1
Parak, F.2
Steigemann, W.3
Petsko, G.A.4
Ponzi, D.R.5
-
29
-
-
0029126458
-
Conformational analysis of endothelin-1: Effects of solvation free energy
-
Hempel, J. C., R. M. Fine, M. Hassan, W. Ghoul, A. Guaragna, S. C. Koerber, Z. Li, and A. T. Hagler. 1995. Conformational analysis of endothelin-1: effects of solvation free energy. Biopolymers. 36:283-301.
-
(1995)
Biopolymers
, vol.36
, pp. 283-301
-
-
Hempel, J.C.1
Fine, R.M.2
Hassan, M.3
Ghoul, W.4
Guaragna, A.5
Koerber, S.C.6
Li, Z.7
Hagler, A.T.8
-
30
-
-
0013787748
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
57
-
-
0023042594
-
Cold denaturation of myoglobin
-
Privalov, P. L., Y. V. Griko, S. Y. Venyaminov, and V. P. Kutyshenko, 1986. Cold denaturation of myoglobin. J. Mol. Biol. 190:487-498.
-
(1986)
J. Mol. Biol.
, vol.190
, pp. 487-498
-
-
Privalov, P.L.1
Griko, Y.V.2
Venyaminov, S.Y.3
Kutyshenko, V.P.4
-
58
-
-
0027250627
-
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
-
59
-
-
0016400371
-
Carbon-13 nuclear magnetic resonance titration shifts in amino acids
-
Quirt, A. R., J. R. J. Lyerla, I. R. Peat, J. S. Cohen, W. F. Reynolds, and M. H. Freedman. 1974. Carbon-13 nuclear magnetic resonance titration shifts in amino acids. J. Am. Chem. Soc. 96:570-574.
-
(1974)
J. Am. Chem. Soc.
, vol.96
, pp. 570-574
-
-
Quirt, A.R.1
Lyerla, J.R.J.2
Peat, I.R.3
Cohen, J.S.4
Reynolds, W.F.5
Freedman, M.H.6
-
60
-
-
0000527952
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
76
-
-
0029364052
-
15N chemical shift referencing in biomolecular NMR
-
15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR. 6:135-140.
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 135-140
-
-
Wishart, D.S.1
Bigam, C.G.2
Yao, J.3
Abildgaard, F.4
Dyson, H.J.5
Oldfield, E.6
Markley, J.L.7
Sykes, B.D.8
-
77
-
-
67650040559
-
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
-
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
-
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
-
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
|