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 Results for DC.creator="C." AND DC.creator="C." AND DC.creator="F." AND DC.creator="Blake" in section 25.1.4 of volume F
Proposals for the catalytic mechanism of lysozyme
Blake, C. C. F., Fenn, R. H., Johnson, L. N., Koenig, D. F., Mair, G. A., North, A. C. T., Oldham, J. W. H., Phillips, D. C., Poljak, R. J., Sarma, V. R. and Vernon, C. A.  International Tables for Crystallography (2012). Vol. F, Section 25.1.4.5, pp. 868-871 [ doi:10.1107/97809553602060000899 ]
... be a hexasaccharide, constructed a hexasaccharide substrate in sites A-F, using the position of the experimentally determined trisaccharide in sites A-C and model building those sugars in sites D-F. Noting also the specificity of lysozyme for bacterial-cell- ...

Binding studies of lysozyme with tri-N-acetyl-chitotriose, (GlcNAc)3, at 2 resolution
Blake, C. C. F., Fenn, R. H., Johnson, L. N., Koenig, D. F., Mair, G. A., North, A. C. T., Oldham, J. W. H., Phillips, D. C., Poljak, R. J., Sarma, V. R. and Vernon, C. A.  International Tables for Crystallography (2012). Vol. F, Section 25.1.4.4, pp. 867-868 [ doi:10.1107/97809553602060000899 ]
... to that occupied by GlcNAc by itself and labelled site C. The acetamido group was visible and fitted neatly into a ... sugars. The free reducing group of the sugar in site C pointed down (towards lower z). The second sugar could ... z), linked to the O4 of the sugar in site C. It was clear that a second tryptophan, Trp62, stacked ...

Low-resolution binding studies of lysozyme with GlcNAc and other sugars
Blake, C. C. F., Fenn, R. H., Johnson, L. N., Koenig, D. F., Mair, G. A., North, A. C. T., Oldham, J. W. H., Phillips, D. C., Poljak, R. J., Sarma, V. R. and Vernon, C. A.  International Tables for Crystallography (2012). Vol. F, Section 25.1.4.3, p. 867 [ doi:10.1107/97809553602060000899 ]
... binding studies were repeated with a number of other compounds (Blake et al., 1967). Kinetic studies using the turbidometric assay ... Sharon) (Fig. 25.1.4.2). Figure 25.1.4.2 | | Inhibitor molecules of lysozyme (Blake et al., 1967). (a) N-acetylglucosamine; (b) N-acetylmuramic acid; (c) 6-iodo-[alpha]-methyl-N-acetylglucosaminide; (d) [alpha]-benzyl- ...

The crystal structure of GlcNAc
Blake, C. C. F., Fenn, R. H., Johnson, L. N., Koenig, D. F., Mair, G. A., North, A. C. T., Oldham, J. W. H., Phillips, D. C., Poljak, R. J., Sarma, V. R. and Vernon, C. A.  International Tables for Crystallography (2012). Vol. F, Section 25.1.4.2, pp. 866-867 [ doi:10.1107/97809553602060000899 ]
... Acta Cryst. 21, 885-891. Johnson, L. N. & Phillips, D. C. (1964). Crystal structure of N-acetylglucosamine. Nature (London), 202, 588-589. Mo, F. & Jensen, L. H. (1975). A refined model for N ... London: Academic Press. International Tables for Crystallography (2012). Vol. F, ch. 25.1, pp. 866-867 International Union of Crystallography ...

Lysozyme substrates
Blake, C. C. F., Fenn, R. H., Johnson, L. N., Koenig, D. F., Mair, G. A., North, A. C. T., Oldham, J. W. H., Phillips, D. C., Poljak, R. J., Sarma, V. R. and Vernon, C. A.  International Tables for Crystallography (2012). Vol. F, Section 25.1.4.1, p. 866 [ doi:10.1107/97809553602060000899 ]
... with the glycosidic bond that is hydrolysed by lysozyme indicated (Blake et al., 1967). The structure is composed of alternating ... 327, 13-20. International Tables for Crystallography (2012). Vol. F, ch. 25.1, p. 866 International Union of Crystallography 2012 | home ...

Structural studies on the biological function of lysozyme
Blake, C. C. F., Fenn, R. H., Johnson, L. N., Koenig, D. F., Mair, G. A., North, A. C. T., Oldham, J. W. H., Phillips, D. C., Poljak, R. J., Sarma, V. R. and Vernon, C. A.  International Tables for Crystallography (2012). Vol. F, Section 25.1.4, pp. 866-871 [ doi:10.1107/97809553602060000899 ]
... with the glycosidic bond that is hydrolysed by lysozyme indicated (Blake et al., 1967). The structure is composed of alternating ... binding studies were repeated with a number of other compounds (Blake et al., 1967). Kinetic studies using the turbidometric assay ... Sharon) (Fig. 25.1.4.2). Figure 25.1.4.2 | | Inhibitor molecules of lysozyme (Blake et al., 1967). (a) N-acetylglucosamine; (b) N- ...

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