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Biophysics and the Challenges of Emerging Threats
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 [...
| Clasificación: | Libro Electrónico |
|---|---|
| Autor Corporativo: | |
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Dordrecht :
Springer Netherlands : Imprint: Springer,
2009.
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| Edición: | 1st ed. 2009. |
| Colección: | NATO Science for Peace and Security Series B: Physics and Biophysics,
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| Temas: | |
| Acceso en línea: | Texto Completo |
MARC
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| 024 | 7 | |a 10.1007/978-90-481-2368-1 |2 doi | |
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| 245 | 1 | 0 | |a Biophysics and the Challenges of Emerging Threats |h [electronic resource] / |c edited by Joseph Puglisi. |
| 246 | 3 | |a Proceedings of the NATO Advanced Study Institute on Biophysics and the Challenges of Emerging Threats Erice, Sicily, Italy 19-30 June 2007 | |
| 250 | |a 1st ed. 2009. | ||
| 264 | 1 | |a Dordrecht : |b Springer Netherlands : |b Imprint: Springer, |c 2009. | |
| 300 | |a VII, 179 p. |b online resource. | ||
| 336 | |a text |b txt |2 rdacontent | ||
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| 490 | 1 | |a NATO Science for Peace and Security Series B: Physics and Biophysics, |x 1874-6535 | |
| 505 | 0 | |a 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. | |
| 520 | |a 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. | ||
| 650 | 0 | |a Life sciences. | |
| 650 | 0 | |a Biophysics. | |
| 650 | 0 | |a Biotechnology. | |
| 650 | 0 | |a Condensed matter. | |
| 650 | 0 | |a Spectrum analysis. | |
| 650 | 0 | |a Chemistry, Physical and theoretical. | |
| 650 | 1 | 4 | |a Life Sciences. |
| 650 | 2 | 4 | |a Biophysics. |
| 650 | 2 | 4 | |a Biotechnology. |
| 650 | 2 | 4 | |a Condensed Matter Physics. |
| 650 | 2 | 4 | |a Spectroscopy. |
| 650 | 2 | 4 | |a Theoretical Chemistry. |
| 700 | 1 | |a Puglisi, Joseph. |e editor. |4 edt |4 http://id.loc.gov/vocabulary/relators/edt | |
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| 776 | 0 | 8 | |i Printed edition: |z 9789048123940 |
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| 830 | 0 | |a NATO Science for Peace and Security Series B: Physics and Biophysics, |x 1874-6535 | |
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| 950 | |a Physics and Astronomy (SpringerNature-11651) | ||
| 950 | |a Physics and Astronomy (R0) (SpringerNature-43715) | ||