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Myoglobin dichroism

Lewis J W, Tilton R F, Einterz C M, Milder S J, Kuntz I D and Kliger D S 1985 New technique for measuring circular dichroism changes on a nanosecond time scale. Application to (carbonmonoxy)myoglobin and (carbonmonoxy)hemoglobin J. Rhys. Chem. 89 289-94... [Pg.2970]

Figure 23-3 Infrared absorbance spectra of the amide regions of proteins. (A) Spectra of insulin fibrils illustrating dichroism. Solid line, electric vector parallel to fibril axis broken line, electric vector perpendicular to fibril axis. From Burke and Rougvie.24 Courtesy of Malcolm Rougvie. See also Box 29-E. (B) Fourier transform infrared (FTIR) spectra of two soluble proteins in aqueous solution obtained after subtraction of the background H20 absorption. The spectrum of myoglobin, a predominantly a-helical protein, is shown as a continuous line. That of concanavalin A, a predominantly (3-sheet containing protein, is shown as a broken line. From Haris and Chapman.14 Courtesy of Dennis Chapman. Figure 23-3 Infrared absorbance spectra of the amide regions of proteins. (A) Spectra of insulin fibrils illustrating dichroism. Solid line, electric vector parallel to fibril axis broken line, electric vector perpendicular to fibril axis. From Burke and Rougvie.24 Courtesy of Malcolm Rougvie. See also Box 29-E. (B) Fourier transform infrared (FTIR) spectra of two soluble proteins in aqueous solution obtained after subtraction of the background H20 absorption. The spectrum of myoglobin, a predominantly a-helical protein, is shown as a continuous line. That of concanavalin A, a predominantly (3-sheet containing protein, is shown as a broken line. From Haris and Chapman.14 Courtesy of Dennis Chapman.
Nicola NA, Minasian E, Appleby CA et al (1975) Circular dichroism studies of myoglobin and leghemoglobin. Biochemistry 14 5141-5149... [Pg.313]

Vickery L, Nozawa T, Sauer K (1976) Magnetic circular dichroism studies of myoglobin complexes. Correlations with heme spin state and axial ligation. J Am Chem Soc 98 343-350... [Pg.313]

Xie X, Simon JD (1990) Picosecond time-resolved circular-dichroism study of protein relaxation in myoglobin following photodissociation of CO. J Am Chem Soc 112 7802-7803... [Pg.235]

Barter M, Guadiano MC, and Santucci R. Influence of Glycerol on the Structure and Stability of Ferric Horse Heart Myoglobin a SAXS and Circular Dichroism... [Pg.390]

M. Sono, A.M. Bracete, A.M. Huff, M. Ikeda-Saito, and J.H. Dawson, Evidence that a formyl-substituted iron porphyrin is the prosthetic group of myeloperoxidase magnetic circular dichroism similarity of the peroxidase to Spirographis heme-reconstituted myoglobin, Proc. Natl. Acad. Sci. USA 88 11148 (1991). [Pg.284]

S. A. Champion, P.M. Determination of CO orientation in myoglobin by single-crystal infrared linear dichroism. J. Am. Chem. Soc. 1994. 116. 4139-4140. [Pg.643]

Recent variable temperature magnetic circular dichroism studies by Foote et al. [219] have shown that the Fe =0 myoglobin derivative exists in two forms, depending on the pH. The observed spectral differences were tentatively ascribed to deprotonation of the proximal histidine at higher pH. [Pg.35]

Sono M, Andersson LA, Dawson JH (1982) Sulfur donor ligand binding to ferric cytochrome P-450-CAM and myoglobin. Ultraviolet-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopic investigation of the complexes. J Biol Chem 257 8308-8320... [Pg.241]

Figure 9.5 Circular dichroism spectra for (A/ sperm whale myoglobin, and (B) concanavalin A. Figure 9.5 Circular dichroism spectra for (A/ sperm whale myoglobin, and (B) concanavalin A.
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See also in sourсe #XX -- [ Pg.58 ]



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