Biophysics and the Challenges of Emerging Threats. 1st ed. 2009

種類:

電子ブック

責任表示:

edited by Joseph Puglisi

出版情報:

Dordrecht : Springer Netherlands : Imprint: Springer, 2009

著者名:

• Puglisi, Joseph.
• SpringerLink (Online service)

シリーズ名:

NATO Science for Peace and Security Series B: Physics and Biophysics ;

ISBN:

9789048123681 [9048123682]    

注記:

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.
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 qu

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