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Detection of new temperature-dependent conformational transition in lysozyme by carbon-13 nuclear magnetic resonance spectroscopy.
Proc Natl Acad Sci U S A. 1975 Jun;72(6):2095-8. doi: 10.1073/pnas.72.6.2095.
2
Comparisons of ring-current shifts calculated from the crystal structure of egg white lysozyme of hen with the proton nuclear magnetic resonance spectrum of lysozyme in solution.
Biochemistry. 1980 Jan 22;19(2):245-58. doi: 10.1021/bi00543a001.
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Effect of chemical modifications at tryptophan-108 on binding of lanthanide ions to hen egg-white lysozyme. Application of natural-abundance carbon-13 nuclear magnetic resonance spectroscopy.
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1H nuclear magnetic resonance studies of hen lysozyme-N-acetylglucosamine oligosaccharide complexes in solution. Application of chemical shifts for the comparison of conformational changes in solution and in the crystal.
J Mol Biol. 1994 Jan 21;235(3):1072-87. doi: 10.1006/jmbi.1994.1058.
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Complete assignment of aromatic 1H nuclear magnetic resonances of the tyrosine residues of hen lysozyme.
Eur J Biochem. 1978 Dec 1;92(1):99-103. doi: 10.1111/j.1432-1033.1978.tb12726.x.
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Studies of chemical modifications of proteins by carbon 13 neuclear magnetic resonance spectroscopy. Reaction of hen egg white lysozyme with iodine.
J Biol Chem. 1976 Nov 10;251(21):6522-8.
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Complete assignment of the 1H NMR spectrum of the aromatic residues of lysozyme.
Eur J Biochem. 1982 Nov 15;128(2-3):527-31. doi: 10.1111/j.1432-1033.1982.tb06997.x.
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Conformational changes, dynamics and assignments in 1H NMR studies of proteins using ring current calculations. Hen egg white lysozyme.
FEBS Lett. 1977 Oct 1;82(1):17-22. doi: 10.1016/0014-5793(77)80876-4.
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Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Relaxation behavior.
J Biol Chem. 1975 Aug 25;250(16):6368-80.
引用本文的文献
1
What's new in lysozyme research? Always a model system, today as yesterday.
Mol Cell Biochem. 1984 Sep;63(2):165-89. doi: 10.1007/BF00285225.
2
Applications of natural-abundance nitrogen-15 nuclear magnetic resonance to large biochemically important molecules.
Proc Natl Acad Sci U S A. 1975 Dec;72(12):4696-700. doi: 10.1073/pnas.72.12.4696.
3
Proton magnetic resonance spectroscopic studies of proteins containing deuterated tryptophan residues.
Mol Cell Biochem. 1976 Nov 30;13(2):113-25. doi: 10.1007/BF01837061.
4
The temperature and pH-dependent transition of hen lysozyme. Characterization of two temperature-defined domains and of an N-acetylglucosamine (inhibitor)-insensitive form.
Mol Biol Rep. 1979 Aug 31;5(3):165-9. doi: 10.1007/BF00778417.
本文引用的文献
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THERMODYNAMICS OF CONFORMATIONAL CHANGES OF PROTEINS. I. PH-DEPENDENT DENATURATION OF MURAMIDASE.
Biochemistry. 1964 Dec;3:1920-8. doi: 10.1021/bi00900a023.
2
The influence of urea on crystallization and polymorphism of hen lysozyme.
FEBS Lett. 1973 Apr 15;31(2):189-192. doi: 10.1016/0014-5793(73)80100-0.
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Calorimetric investigation of lysozyme thermal denaturation.
FEBS Lett. 1973 Feb 15;30(1):57-60. doi: 10.1016/0014-5793(73)80618-0.
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Nuclear magnetic resonance study of the mechanism of reversible denaturation of lysozyme.
J Am Chem Soc. 1971 Jan 13;93(1):235-46. doi: 10.1021/ja00730a039.
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Carbon-13 Fourier transform nuclear magnetic resonance. II. Ribonuclease.
Proc Natl Acad Sci U S A. 1970 Nov;67(3):1093-6. doi: 10.1073/pnas.67.3.1093.
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Crystallization of a multienzyme complex: fatty acid synthetase from yeast.
Proc Natl Acad Sci U S A. 1969 Aug;63(4):1377-82. doi: 10.1073/pnas.63.4.1377.
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High temperature crystallization of lysozyme: an example of phase transition.
FEBS Lett. 1972 Jun 1;23(1):21-3. doi: 10.1016/0014-5793(72)80273-4.
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Crystallization with hapten of the Fab' fragment from a mouse IgA myeloma protein with antidinitrophenyl activity.
J Biol Chem. 1971 Oct 25;246(20):6272-5.
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Fluctuation of the lysozyme structure. II. Effects of temperature and binding of inhibitors.
J Mol Biol. 1973 Apr 25;75(4):673-82. doi: 10.1016/0022-2836(73)90300-8.
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Natrual-abundance carbon-13 nuclear magnetic resonance studies in 20-mm sample tubes. Observation of numerous single-carbon resonances of hen egg-white lysozyme.
Biochemistry. 1973 Mar 27;12(7):1335-41. doi: 10.1021/bi00731a013.
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