Biophysics and the Challenges of Emerging Threats

• Συγγραφή απο Οργανισμό/Αρχή: SpringerLink (Online service)
• Άλλοι συγγραφείς: Puglisi, Joseph D. (Επιμελητής έκδοσης)
• Μορφή: Ηλεκτρονική πηγή Ηλ. βιβλίο
• Γλώσσα: English
• Έκδοση: Dordrecht : Springer Netherlands, 2009.
• Σειρά: NATO Science for Peace and Security Series B: Physics and Biophysics,
• Θέματα: Life sciences.; Biotechnology.; Chemistry, Physical and theoretical.; Solid state physics.; Biophysics.; Biological physics.; Spectroscopy.; Microscopy.; Life Sciences.; Life Sciences, general.; Biophysics and Biological Physics.; Solid State Physics.; Spectroscopy and Microscopy.; Theoretical and Computational Chemistry.

 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. 

 A Simple Model for Protein Folding -- Complementarity of Hydrophobic/Hydrophilic Properties In Protein—Ligand Complexes: A New Tool to Improve Docking Results -- Structures of Cvnh Family Lectins -- Biophysical Approaches To Study Dna Base Flipping -- The Diversity of Nuclear Magnetic Resonance Spectroscopy -- Improved Dye Stability in Single-Molecule Fluorescence Experiments -- The Evaluation of Isotope Editing and Filtering for Protein—Ligand Interaction Elucidation by Nmr -- Ribosome: an Ancient Cellular Nano-Machine for Genetic Code Translation.