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Proteins, fluorescence mobility

Quenching studies of protein fluorescence provide answers regarding the accessibility of certain internal or external groups to quencher molecules. Another application concerns the study of associative behavior and properties of proteins and membranes. The rationale is that the fluorescence transition is polarized and this polarization can be exploited in time-resolved analysis and interpreted in terms of the rotation or tumbling motion which in turn is determined by the viscosity and structure of the environment of the fluorescing group. In particular, anisotropy decay studies have yielded a great deal of information on the mobility of natural and artificial membranes and/or the dynamics of proteins as well as small molecules in membranes. For such studies fluorescence lifetime labels that can be attached to proteins or that dissolve in membranes have... [Pg.340]

At present, there is widespread interest in directly measuring the time-dependent processes. This is because considerably more information is av lilable from the time-dependent data. For example, the time-dependent decays of protein fluorescence can occasionally be used to recover the emission spectra of individual tryptophan residues in a protein. The time-resolved anisotropies can reveal the shape of the protein and/or the extent of residue mobility within the protein. The time-resolved energy transfer can reveal not only the distance between the donor and acceptor, but also the distribution of these distances. The acquisition of such detailed information requires high resolution instrumentation and careful data acquisition and analysis. [Pg.14]

Corbett, J. D. Cho, M. R. Golan, D. E. Deoxygenation affects fluorescence photobleaching recovery measurements of red cell membrane protein lateral mobility. Biophys. J. 1994,66,25-30. [Pg.225]

Fluorescence is also a powerful tool for investigating the structure and dynamics of matter or living systems at a molecular or supramolecular level. Polymers, solutions of surfactants, solid surfaces, biological membranes, proteins, nucleic acids and living cells are well-known examples of systems in which estimates of local parameters such as polarity, fluidity, order, molecular mobility and electrical potential is possible by means of fluorescent molecules playing the role of probes. The latter can be intrinsic or introduced on purpose. The high sensitivity of fluo-rimetric methods in conjunction with the specificity of the response of probes to their microenvironment contribute towards the success of this approach. Another factor is the ability of probes to provide information on dynamics of fast phenomena and/or the structural parameters of the system under study. [Pg.393]

J. R. Lakowicz and G. Weber, Nanosecond segmental mobilities of tryptophan residues in proteins observed by lifetime-resolved fluorescence anisotropies, Biophys. J. 32, 591-601 (1980). [Pg.109]

A. P. Demchenko, On the nanosecond mobility in proteins. Edge excitation fluorescence red... [Pg.110]

Lorenz, M., Hillisch, A., Payet, D., Buttinelli, M., Travers, A., and Diekmann, S. (1999) DNA bending induced by high mobility group proteins studied by fluorescence resonance energy transfer. Biochemistry 38, 12150-12158. [Pg.126]

Fig. 10 Binding curves obtained by measuring the electrophoretic mobility ( ) and fluorescence anisotropy (o) of F-ll-mer at varying concentrations of SSB protein in the running buffer. Conditions were the same as for Figure 9. (From Ref. 48.)... Fig. 10 Binding curves obtained by measuring the electrophoretic mobility ( ) and fluorescence anisotropy (o) of F-ll-mer at varying concentrations of SSB protein in the running buffer. Conditions were the same as for Figure 9. (From Ref. 48.)...

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See also in sourсe #XX -- [ Pg.3 ]

See also in sourсe #XX -- [ Pg.3 ]




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