High impact information on Optical Rotatory Dispersion

• These measurements, in concert with optical rotatory dispersion spectroscopy, established that, for optically pure cyclophosphamide, [alphaD] = 2.3 +/- 0.2 degrees [1].
• The optical rotatory dispersion spectrum of apohemoglobin is also modified by its interaction with inositol hexaphosphate suggesting a small increase in the helical content of the protein [2].
• Spectrofluorescence and optical rotatory dispersion measurements show that there is no detectable conformational change for the guanidinated phosphoglycerate kinase and that there are slight changes in the spectra suggesting that there may be slight conformational changes for the nitrotroponylated and the pyridoxal phosphate-modified enzymes [3].
• In a previous study (Chemical Physics Letters 2005, 401 , 385) we computed the optical rotatory dispersion of (S)-propylene oxide in gas phase and solution using the hierarchy of coupled cluster models CCS, CC2, CCSD, and CC3 [4].
• The folding dynamics of reduced cytochrome c (redcyt c) obtained from tuna heart, which contains a tryptophan residue at the site occupied by His33 in horse heart cytochrome c, was studied using nanosecond time-resolved optical rotatory dispersion spectroscopy [5].

Biological context of Optical Rotatory Dispersion

• The kinetics of helix unfolding of an azobenzene cross-linked peptide probed by nanosecond time-resolved optical rotatory dispersion [6].

Associations of Optical Rotatory Dispersion with chemical compounds

• In the study of proteins, the circular polarization of luminescence yields more specific information than circular dichroism or optical rotatory dispersion since nonfluorescent chromophores do not contribute, and the spectra of the tyrosine and the tryptophan residues are much better resolved in emission than in absorption [7].
• By contrast, the apomyoglobin-protoporphyrin IX complex does not react with Bromophenol Blue. 6. Optical-rotatory-dispersion measurements show that the laevorotation of apomyoglobin is increased towards that of metmyglobin in the presence of haemin and protoporphyrin IX [8].
• The C-1 to C-3 fragment of each isolated [2-2H]-D-gluco-octulose product was recovered as [2-2H]propionic acid and identified by its positive optical rotatory dispersion as the S isomer, showing that each enzyme had protonated the octenitol (at C-2) from above its re face [9].
• 3. The optical absorption, optical-rotatory-dispersion and circular-dichroism spectra are typical of ferredoxins containing 4Fe-4S clusters [10].
• It was shown by optical-rotatory-dispersion spectrum and optical-resolution h.p.l.c. analysis that this compound consisted of equimolar amounts of D-aspartic acid and glycine [11].

Gene context of Optical Rotatory Dispersion

• Circular dichroism, optical rotatory dispersion, and absorption studies on the conformation of bovine rhodopsin iw situ and solubilized with detergent [12].
• Optical rotatory dispersion in the visible region failed to show the presence of pronounced secondary structures in the reduced BPTI and no binding of 8-anilino-1-naphthalenesulphonic acid to reduced BPTI could be detected [13].
• The absolute stereochemistry of the three active centers was determined to be RRR by optical rotatory dispersion comparisons [14].

Analytical, diagnostic and therapeutic context of Optical Rotatory Dispersion

• Circular dichroism, optical rotatory dispersion, and difference uv spectra all indicate the purified protein to undergo a conformational transition upon forming a complex with a steroid ligand [15].
• Electron microscopy and optical rotatory dispersion (ORD) show that sterols disperse with cerebrosides and gangliosides to form cylindrical structures with the regions around C atoms 3 and 7 of the sterol in less polar environments than those they occupy in phospholipid liposomes [16].

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