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Myoglobin diffraction

As described in Chapter 2, the first complete protein structure to be determined was the globular protein myoglobin. However, the a helix that was recognized in this structure, and which has emerged as a persistent structural motif in the many hundreds of globular proteins determined subsequently, was first observed in x-ray diffraction studies of fibrous proteins. [Pg.384]

Fig. 7. The instrumental set up at XI1 /DORIS for time resolved data collection with a linear detector for CO myoglobin following laser photolysis of the ligand. A section of the diffraction pattern with stationary crystal, stationary detector is recorded with a linear detector and (b) shows the time course of three reflections before and after the laser flash (from Bartunik et al. 1982)... Fig. 7. The instrumental set up at XI1 /DORIS for time resolved data collection with a linear detector for CO myoglobin following laser photolysis of the ligand. A section of the diffraction pattern with stationary crystal, stationary detector is recorded with a linear detector and (b) shows the time course of three reflections before and after the laser flash (from Bartunik et al. 1982)...
Dadusc, G., Ogilvie, J. R, Schulenberg, R, Marvet, U., and Miller, R. J. D. 2001. Diffractive optics-based heterodyne-detected four-wave mixing signals of protein motion From protein quakes to ligand escape for myoglobin. Proc. Nat. Acad. Sci. USA 98 6110-6115. [Pg.29]

Srajer, V., Ren, Z., Teng, T. Y., Schmidt, M., Ursby, T., Bourgeois, D., Pradervand, C., Schildkamp, W., Wulff, M., and Moffat, K. 2001. Protein conformational relaxation and ligand migration in myoglobin Nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction. Biochemistry 40 13802-15. [Pg.32]

John Kendrew found that the x-ray diffraction pattern of crystalline myoglobin (isolated from muscles of the sperm whale) is very complex, with nearly 25,000 reflections. Computer analysis of these reflections took place in stages. The resolution improved at each stage, until in 1959 the positions of virtually all the non-hydrogen atoms in the protein had been determined. The amino acid sequence of the protein, obtained by chemical analysis, was consistent with the molecular model. The structures of thousands of proteins, many of them much more complex than myoglobin, have since been determined to a similar level of resolution. [Pg.137]

Globular proteins have more complicated tertiary structures, often containing several types of secondary structure in the same polypeptide chain. The first globular protein structure to be determined, using x-ray diffraction methods, was that of myoglobin. [Pg.146]

The first protein structure to be learned was that of myoglobin, which was established by Kendrew et al. in I960.391-393 That of the enzyme lysozyme was deduced by Blake et al. in 1965.394 Since then, new structures have appeared at an accelerating rate so that today we know the detailed architecture of over 6000 different proteins395 with about 300 distinctly different folding patterns 396 New structures are being determined at the rate of about one per day. X-ray diffraction has also been very important to the study of naturally or artifically oriented fibrous proteins397 and provided the first experimental indications of the P structure of proteins. [Pg.133]

X-Ray diffraction data of high resolution are available for a number of hemoglobins and myoglobins, due to the work of Perutz and Kendrew and their colleagues. [Pg.685]

For an example of Laue diffraction applied to time-resolved crystallography, see V. Srajer, T. Teng, T. Ursby, C. Pradervand, Z. Ren, S. Adachi, W. Schildkamp, D. Bourgeois, M. Wulff, and K. Moffat, Photolysis of the carbon monoxide complex of myoglobin Nanosecond time-resolved crystallography, Science 274, 1726-1729, 1996. [Pg.213]


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See also in sourсe #XX -- [ Pg.103 ]




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