By A. D. McLaren, P. Alexander, Z. M. Bacq, D. Shugar
Photochemistry of Proteins and Nucleic Acids specializes in the consequences of ultraviolet and visual radiations on proteins and nucleic acids. The ebook first discusses a few rules of photochemistry, together with the legislation of photochemistry and components influencing photochemical reactions in ideas. The textual content describes absorption and luminescence spectra of nucleoproteins and their elements, together with critical soaking up teams in proteins, nucleic acids, and nucleoproteins. the choice additionally highlights the motion of ultraviolet mild on proteins; photochemical and photosensitized inactivation of enzymes; and the photochemistry of purine and pyrimidine derivatives. The textual content additionally discusses nucleic acids and oligo- and polynucleotides. subject matters contain photochemical degradation of nucleic acid; kinetics of organic inactivation of nucleic acids; nucleoproteins; and reversibility of nucleic acid photolysis. The publication additionally encompasses the inactivation of viruses, together with inactivation reviews with a plant virus, bacteriophages, and photochemically produced vaccines. The textual content additionally offers a few difficulties in photobiology and a few thoughts in photochemistry. The textual content is an effective resource of knowledge for readers drawn to the learn of proteins and nucleic acids.
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Extra info for Photochemistry of Proteins and Nucleic Acids
O n the other hand most of the evidence adduced by Schauenstein et al. for peptenol absorption is, as mentioned above, based on studies of oriented fibrous proteins and hence also of the ultraviolet dichroism associated with them. T h e existence of such chromophores in vivo is conceivable and, since their absorption m a x i m u m is in the neighborhood of 2500 A, would be of considerable significance in photochemical studies on living organisms inasmuch as most of such work is done at 2537 Ä. More recently Schauenstein et al.
2-1 exhibits the spectra of tryptophan, tyrosine, phenylalanine, FIG. 2-1. Absorption spectra at neutral pH of tryptophan (a), tyrosine (b), phenylalanine (c), cystine (d) and cysteine (e). cystine, and cysteine, all at neutral pH, plotted as molar extinction coefficients on the same scale so as to give a representative picture of the relative contribution of each to the spectrum of a given protein. Cysteine deserves special mention at this point because of the fact that, until very recently, it had been practically ignored, its extinction having been assumed to be negligible on the basis of measurements made in acid medium.
CHAPTER II Absorption and Luminescence Spectra of Nucleoproteins and their Components REFERENCE has already been made in the previous chapter to the importance of an adequate knowledge of absorption spectra, and associated absorbing structures, in attempts to interpret the nature of a photochemical reaction. It must now be emphasized that this is all the more important with respect to proteins and nucleic acids inasmuch as the absorption spectra of these substances and their derivatives are very frequently used for following the effects of radiation as well as the nature of the resulting photoproducts.