modify your search
 Results for DC.creator="D." AND DC.creator="C." AND DC.creator="Phillips" 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 ]
... s work had shown that the hydrolysis of methyl-[alpha]-D-glucopyranoside proceeded via a ring-closed carbonium-ion intermediate (i.e. ... 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- ...

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 ]
... cleft in the enzyme surface between the two domains (Johnson & Phillips, 1965). The power of the difference-Fourier technique in ... al., 1967). (a) N-acetylglucosamine; (b) N-acetylmuramic acid; (c) 6-iodo-[alpha]-methyl-N-acetylglucosaminide; (d) [alpha]-benzyl-N-acetylmuramic acid; (e) di-N-acetylchitobiose; ( ...

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 ]
... 1962-1964), LNJ determined the crystal structure of GlcNAc. [beta]-D-N-Acetylglucosamine was crystallized from a methanol-water mixture, and ... of the N-acetyl group normal to the ring (Johnson & Phillips, 1964; Johnson, 1966). The structure of glucosamine hydrochloride had ... N. (1966). The crystal structure of N-acetyl-[alpha]-D-glucosamine. Acta Cryst. 21, 885-891. Johnson, L. N. & ...

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 ]
Lysozyme substrates 25.1.4.1. Lysozyme substrates By the summer of 1964, the results for the structure determination of lysozyme were sufficiently promising for us to consider diffraction studies on the biological function of lysozyme. At about the same time, the Royal Society invited Max Perutz to organise a Discussion Meeting on lysozyme ...

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 ]
... 1962-1964), LNJ determined the crystal structure of GlcNAc. [beta]-D-N-Acetylglucosamine was crystallized from a methanol-water mixture, and ... of the N-acetyl group normal to the ring (Johnson & Phillips, 1964; Johnson, 1966). The structure of glucosamine hydrochloride had ... cleft in the enzyme surface between the two domains (Johnson & Phillips, 1965). The power of the difference-Fourier technique ...

powered by swish-e
























































to end of page
to top of page