A combined experimental and theoretical study of optical rotatory dispersion for (R)-glycidyl methyl ether in aqueous solution

2019 ◽  
Vol 21 (7) ◽  
pp. 3644-3655 ◽  
Author(s):  
Franco Egidi ◽  
Tommaso Giovannini ◽  
Gianluca Del Frate ◽  
Paul M. Lemler ◽  
Patrick H. Vaccaro ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Experimental Study ◽  
Methyl Ether ◽  
Solvent Effects ◽  
Theoretical Study ◽  
Optical Rotation ◽  
Classical Model ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Optical Rotatory

We present a theoretical-experimental study of the optical rotation of (R)-glycidylmethylether using a mixed quantum-classical model for solvent effects.

scholarly journals The formula for the optical rotatory dispersion of quartz

1929 ◽  
Vol 122 (789) ◽  
pp. 245-250 ◽  
Keyword(s):  
Original Work ◽  
Optical Rotation ◽  
Ultra Violet ◽  
Original Method ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Optical Rotatory ◽  
Infra Red

The optical rotation of quartz has been measured over a large band of wavelengths. We have Gumlich’s original work over the range from λ = 2·140 μ to λ = 0·21935 μ , repeated and extended into the ultra-violet by Soret and Sarasin and Guye. More recently a series of accurate measurements covering the same range was published by Lowry, and then Duclaux and Jeantet gave a series of results for a range in the ultra-violet from λ = 0·30876 μ to λ = 0·1853980 μ . Finally, Lowry and Coode-Adams, having improved the accuracy of their original method, succeeded in obtaining a very accurate set of readings extending from λ = 2·5170 μ in the infra-red to λ = 0·2280 μ in the ultra-violet, reaching thus just up to the region measured by Duclaux and Jeantet. Various attempts have been made to fit these results into a formula. Gumlich found it possible to represent his results by a formula of the type ω = α 1 /λ 2 + α 2 /λ 4 + α 3 /λ 6 + α 4 /λ 8 + α 5 /λ 10 , but Kettler had almost equal success with the simpler form ω = (λ 2 α)/β.

Some features of the optical rotatory dispersion spectrum of the α-lytic protease of Sorangium sp.

1969 ◽  
Vol 47 (3) ◽  
pp. 317-321 ◽  
Author(s):  
G. M. Paterson ◽  
D. R. Whitaker
Keyword(s):  
Optical Rotation ◽  
Substrate Binding ◽  
Cotton Effect ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Kinetic Properties ◽  
Optical Rotatory ◽  
Cotton Effects ◽  
Ph Dependent

A study of the kinetic properties of the α-lytic protease of Sorangium sp. indicated that substrate-binding by the enzyme was not pH dependent. In agreement with this indication of a pH-insensitive conformation, the optical rotation of the enzyme between pH 5 and 10.5 is not pH dependent. The optical rotatory dispersion spectrum above 220 mμ shows a main Cotton effect with a trough at 230 mμ and small but well-marked Cotton effects between 260 and 300 mμ. The reduced, mean residue rotation at the trough of the main Cotton effect was estimated to be −1650 ± 80° cm2/dmole; the Moffitt–Yang parameter b0 for rotations above 325 mμ is approximately zero. These values suggest that the enzyme has virtually no α-helices.

scholarly journals The Conformation of a Soluble Wool Keratin Derivative

1963 ◽  
Vol 16 (1) ◽  
pp. 231 ◽  
Author(s):  
BS Harrap
Keyword(s):  
Aqueous Solution ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Random Coil ◽  
Optical Rotatory ◽  
Upper Limit ◽  
Helical Content ◽  
Degree Of Severity ◽  
Wool Keratin

The conformation of a low-sulphur soluble wool keratin derivative (SCMKA) has been studied by optical rotatory dispersion. On the assumption that the overall conformation consists of a mixture of a-helical and random-coil regions, this protein has a helical content of about 50% in aqueous solution at pH 9�1; this helical content does not vary with the degree of severity of the preparative procedure. The protein may be reversibly converted to the random-coil form by heating to 70�0, or by treatment with urea at concentrations exceeding 6r.r. An increase in pH to 12�5 causes very little change in conformation, such change as does occur being reversible. The maximum helical content which has been induced by solvents into the protein is about 62% in 2-chloroethanol. This probably represents the upper limit of the helical content of this protein as it occurs in the fibre. The changes in the conforma. tion of the protein which occur in several other solvents are briefly discussed.

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