Optical rotatory dispersion of N-(2-pyridyl N-oxide)amino-acids: empirical correlation of cotton effect with chromophoric substituents

1967 ◽  
pp. 321
Author(s):  
V. Tortorella ◽  
G. Bettoni
Keyword(s):  
Amino Acids ◽  
Cotton Effect ◽  
Empirical Correlation ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Optical Rotatory

Optical Rotatory Dispersion of L-Amino Acids in Acid Solution*

Biochemistry ◽  
1964 ◽  
Vol 3 (10) ◽  
pp. 1519-1524 ◽  
Author(s):  
Eisaku Iizuka ◽  
Jen Tsi Yang
Keyword(s):  
Amino Acids ◽  
Acid Solution ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Optical Rotatory

scholarly journals Study on the Optical Rotatory Dispersion of Di-Peptides and its Application to the Recognition of Di-Peptides from Higher Peptides and Amino Acids

1968 ◽  
Vol 32 (4) ◽  
pp. 518-521 ◽  
Author(s):  
Hiroshi MEGURO ◽  
Toshio KONNO ◽  
Hiroyuki SHIRAISHI ◽  
Eisuke MUNEKATA ◽  
Katura TUJIMURA
Keyword(s):  
Amino Acids ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Optical Rotatory

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.

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