Tryptophan Raman spectroscopy

This enzyme [EC 1.4.99.3], also known as amine dehydrogenase and primary-amine dehydrogenase, catalyzes the reaction of R-CH2-NH2 with water and an acceptor to produce R-CHO, ammonia, and the reduced acceptor. Tryptophan tryptophylquinone (TTQ) is the cofactor for this enzyme. See Resonance Raman Spectroscopy Topaquinone... 

UV resonance Raman spectroscopy (UVRR), Sec. 6.1, has been used to determine the secondary structure of proteins. The strong conformational frequency and cross section dependence of the amide bands indicate that they are sensitive monitors of protein secondary structure. Excitation of the amide bands below 210 nm makes it possible to selectively study the secondary structure, while excitation between 210 and 240 nm selectively enhances aromatic amino acid bands (investigation of tyrosine and tryptophan environments) (Song and Asher, 1989 Wang et al., 1989, Su et al., 1991). Quantitative analysis of the UVRR spectra of a range of proteins showed a linear relation between the non-helical content and a newly characterized amide vibration referred to as amide S, which is found at 1385 cm (Wang et al., 1991). 

Backes, G., Davidson, V. L., Huitema, F., Duine, J. A., and Sanders-Loehr, J., 1991, Characterization of the tryptophan-derived quinone cofactor of methylamine dehydrogenase by resonance Raman spectroscopy, Biochemistry 30 9201n9210. 

NMR results for gramicidin A incorporated into oriented DMPC bilayers produced results that were interpreted as being consistent with the structure of gramicidin A incorporated into SDS micelles (i.e. no tryptophan 9/15 stacking). The results of a Raman spectroscopy study of water accessibility to the tryptophan indole NH sites of gramicidin A incorporated into a hposome (dilauroyl-L-a-phosphatidylchoUne) aqueous suspension were interpreted as being consistent with the stacked tryptophan structure. Obviously, the... 

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