| 期刊全称 | Biophysics and the Challenges of Emerging Threats | | 影响因子2023 | Joseph D. Puglisi | | 视频video | | | 发行地址 | Presents state of the art information on NMR spectroscopy, and its place in the broader field of biophysics.No other monograph presents such a wide range of topics, including NMR spectroscopy, protein | | 学科分类 | NATO Science for Peace and Security Series B: Physics and Biophysics | | 图书封面 |  | | 影响因子 | 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 | | Pindex | Conference proceedings 2009 |
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发表于 2025-3-21 19:36:30
