Biophysics and the challenges of emerging threats [electronic resource] / edited by Joseph D. Puglisi.
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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Format: | Electronic Conference Proceeding eBook |
Language: | English |
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Series: | NATO Science for Peace and Security series. Physics and biophysics.
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MARC
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245 | 1 | 0 | |a Biophysics and the challenges of emerging threats |h [electronic resource] / |c edited by Joseph D. Puglisi. |
260 | |a Dordrecht : |b Springer, |c ©2009. | ||
300 | |a 1 online resource (vii, 179 pages) : |b illustrations. | ||
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490 | 1 | |a NATO science for peace and security series. Series B, Physics and biophysics. | |
500 | |a Selected conference papers. | ||
504 | |a Includes bibliographical references and index. | ||
505 | 0 | |a A simple model for protein folding / Eric R. Henry and William A. Eaton -- Complementarity of hydrophobic/hydrophilic properties in protein-Ligand complexes: a new tool to improve docking results / Timothy V. Pyrkov [and others] -- Structures of Cvnh family lectins / Angela M. Gronenborn -- Biophysical approaches to study DNA base flipping / Saulius Klimasauskas, Zita Liutkeviciute and Dalia Daujotyte -- The diversity of nuclear magnetic resonance spectroscopy / Corey W. Liu [and others] -- Improved dye stability in single-molecule fluorescence experiments / Colin Echeverria Aitken, R. Andrew Marshall and Joseph D. Pugi -- The evaluation of isotope editing and filtering for protein-Ligand interaction elucidation by Nmr / Ian M. Robertson, Leo Spyracopoulos and Brian D. Sykes -- Ribosome: an ancient cellular nano-machine for genetic code translation / Ada Yonath. | |
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. |0 http://id.loc.gov/authorities/names/no2005095743 |1 http://isni.org/isni/0000000109750535. | |
776 | 0 | 8 | |i Print version: |a NATO Advanced Study Institute on Biophysics and the Challenges of Emerging Threats (2007 : Erice, Italy). |t Biophysics and the challenges of emerging threats. |d Dordrecht : Springer, ©2009 |z 9789048123667 |z 9048123666 |w (OCoLC)310400976. |
830 | 0 | |a NATO Science for Peace and Security series. |n B, |p Physics and biophysics. |0 http://id.loc.gov/authorities/names/no2007112607. | |
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