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 [...
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| Tác giả chính: | |
|---|---|
| Định dạng: | Livre numérique |
| Ngôn ngữ: | Anglais |
| Được phát hành: |
Dordrecht :
Springer Netherlands
[20..].
Cham : Springer Nature |
| Phiên bản: | 1st ed. 2009. |
| Loạt: | NATO Science for Peace and Security Series B: Physics and Biophysics
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| Những chủ đề: | |
| Truy cập trực tuyến: | Accès sur la plateforme de l'éditeur Accès sur la plateforme Istex Accès Université d'Orléans Accès INSA CVL |
| Chú thích: |
Archives Springer e-books (Licence nationale) Archives Springer e-books (Licence nationale) |
| Autres localisations: | Voir dans le Sudoc |
| Variante du titre: | Proceedings of the NATO Advanced Study Institute on Biophysics and the Challenges of Emerging Threats Erice, Sicily, Italy 19-30 June 2007 |
| Edition sous un autre format: | • Biophysics and the challenges of emerging threats, [proceedings of the NATO advanced study institute on Biophysics and the challenges of emerging threats, Erice, Scily, Italy, 19-30 june 2007], edited by Joseph D. Puglisi, Dordrecht, Springer, 2009, 1 vol. (VII-179 p.), NATO science for peace and security series, 978-90-481-2366-7 |
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| 240 | 1 | 0 | |a Proceedings of the NATO Advanced Study Institute on Biophysics and the Challenges of Emerging Threats Erice, Sicily, Italy 19-30 June 2007 |
| 245 | 0 | 0 | |a Biophysics and the Challenges of Emerging Threats |c edited by Joseph D. Puglisi. |
| 250 | |a 1st ed. 2009. | ||
| 260 | |a Dordrecht : |b Springer Netherlands. | ||
| 260 | |a Cham : |b Springer Nature, |c [20..]. | ||
| 490 | 0 | |a NATO Science for Peace and Security Series B: Physics and Biophysics |x 1874-6535 | |
| 500 | |a Archives Springer e-books (Licence nationale) | ||
| 500 | |a Archives Springer e-books (Licence nationale) | ||
| 505 | 1 | |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 | |
| 506 | |a Accès en ligne pour les établissements français bénéficiaires des licences nationales | ||
| 506 | |a Accès soumis à abonnement pour tout autre établissement | ||
| 506 | |a Conditions particulières de réutilisation pour les bénéficiaires des licences nationales. https://www.licencesnationales.fr/springer-nature-ebooks-contrat-licence-ln-2017 | ||
| 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 | ||
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| 700 | 1 | |a Puglisi, Joseph D. |4 aut | |
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