Biophysics and the Challenges of Emerging Threats (NATO Science for Peace and Security Series B: Physics and Biophysics)

Joseph Puglisi

ISBN 10: 9048123674 / ISBN 13: 9789048123674

Editore: Springer 2009-06-05, 2009

Riguardo questo articolo

Codice articolo 6666-IUK-9789048123674

Dati bibliografici

• Titolo: Biophysics and the Challenges of Emerging Threats (NATO Science for Peace and Security Series B: Physics and Biophysics)
• Editore: Springer 2009-06-05
• Data di pubblicazione: 2009
• Lingua: Inglese
• ISBN 10: 9048123674
• ISBN 13: 9789048123674
• Rilegatura: Paperback
• Condizione: New

Descrizione articolo

Riassunto

Single-molecule techniques eliminate ensemble averaging, thus revealing transient or rare species in heterogeneous systems [1–3]. These approaches have been employed to probe myriad biological phenomena, including protein and RNA folding [4–6], enzyme kinetics [7, 8], and even protein biosynthesis [1, 9, 10]. In particular, immobilization-based fluorescence te- niques such as total internal reflection fluorescence microscopy (TIRF-M) have recently allowed for the observation of multiple events on the millis- onds to seconds timescale [11–13]. Single-molecule fluorescence methods are challenged by the instability of single fluorophores. The organic fluorophores commonly employed in single-molecule studies of biological systems display fast photobleaching, intensity fluctuations on the millisecond timescale (blinking), or both. These phenomena limit observation time and complicate the interpretation of fl- rescence fluctuations [14, 15]. Molecular oxygen (O) modulates dye stability. Triplet O efficiently 2 2 quenches dye triplet states responsible for blinking. This results in the for- tion of singlet oxygen [16–18]. Singlet O reacts efficiently with organic dyes, 2 amino acids, and nucleobases [19, 20]. Oxidized dyes are no longer fluor- cent; oxidative damage impairs the folding and function of biomolecules. In the presence of saturating dissolved O , blinking of fluorescent dyes is sup- 2 pressed, but oxidative damage to dyes and biomolecules is rapid. Enzymatic O -scavenging systems are commonly employed to ameliorate dye instability. 2 Small molecules are often employed to suppress blinking at low O levels.

Contenuti

Preface.- List of Contributors.- A Simple Model for Protein Folding; E.R. Henry, W.A. Eaton.- Complementarity of Hydrophobic/Hydrophilic Properties in Protein Ligand Complexes: A New Tool to Improve Docking Results; T.V. Pyrkov et al.- Structures of Cvnh Family Lectins; A.M. Gronenborn.- Biohysical Approaches to Study DNA Base Flipping; S. Klimasauskas et al.- The Diversity of Nuclear Magnetic Resonance Spectroscopy; C.W. Liu.- Improved Dye Stability in Single-Molecule Fluorescence Experiments; C.E. Aitken et al.- The Evaluation of Isotope Editing and Filtering for Protein-Ligand Interaction Elucidation by NMR; I.M. Robertson et al.- Ribosome: an Ancient Cellular Nano-Machine for Genetic Code Translation; A. Yonath.- Course Abstracts and Posters.- Author Index.-