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" Biophysics and the challenges of emerging threats / "
edited by Joseph D. Puglisi.
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BL
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| Record Number
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955926
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b710296
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| Main Entry
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NATO Advanced Study Institute on Biophysics and the Challenges of Emerging Threats(2007 :, Erice, Italy)
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| Title & Author
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Biophysics and the challenges of emerging threats /\ edited by Joseph D. Puglisi.
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| Publication Statement
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Dordrecht :: Springer,, ©2009.
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| Series Statement
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NATO science for peace and security series. Series B, physics and biophysics
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| Page. NO
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1 online resource (vii, 179 pages) :: illustrations
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| ISBN
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9048123682
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: 9789048123681
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9048123666
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9048123674
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9789048123667
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9789048123674
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| Notes
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Selected conference papers.
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| Bibliographies/Indexes
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Includes bibliographical references and index.
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| Contents
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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.
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| Abstract
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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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Biophysics, Congresses.
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Bioterrorism, Congresses.
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Biophysics.
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Bioterrorism.
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Physique.
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Biophysics.
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Bioterrorism.
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| Dewey Classification
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571.4
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| LC Classification
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QH505.P76 2009
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| NLM classification
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2009 M-170
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QT 34N2795b 2008
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D815. 5-05clc
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Q6-532clc
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| Added Entry
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Puglisi, Joseph D.
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