Titlebook: Ultraviolet Spectroscopy of Proteins; Alexander P. Demchenko Book 1986 Springer-Verlag Berlin Heidelberg 1986 Photometer.UV.biochemistry.b

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Fluorescence Molecular Relaxation Spectroscopy,, to structural changes in proteins. However, this method has not yet been developed to the extent of enabling a strict and unequivocal interpretation of protein structure, based on the spectra under study. Despite great research effort and an enormous amount of accumulated experimental data, we sti

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insincerity

Fluorescence Polarization and Rotational Mobility,olarization. If characteristic times of Brownian rotation are comparable in magnitude with fluorescence lifetime, the size and, sometimes, the shape of the molecule or its mobile segment can be estimated by measuring the fluorescence polarization. The first variant of this method, suggested by Weber

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Intrinsic Phosphorescence of Proteins,well as of conformational analysis of protein macromolecules. In recent years, many specialists have been displaying a keen interest for phosphorescence which is a spin-forbidden emissive transition of a molecule from the excited triplet state to the ground singlet one. The lifetime of phosphorescen

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Employment of Ultraviolet Spectroscopy in Analytical Chemistry of Proteins,requently employed in the examination of highly purified protein preparations and frac-tional distribution of proteins. Such methods have the important advantage that the sample remains intact and can be used for further investigations. Spectrophotometric analysis of proteins can be carried out unde

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enhance

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Spectroscopic Properties of Protein Chromophores,nges are used for conducting experiments in protein spectroscopy. In emission spectra the contribution of the tryptophan chromophore is the most important one. A detailed description of spectroscopic properties of chromophores composing the protein molecule and their analogs is given below.