| Description |
1 online resource (vii, 179 pages) : illustrations |
| Series |
NATO science for peace and security series. Series B, physics and biophysics |
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NATO Science for Peace and Security series. B, Physics and biophysics.
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| Contents |
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 |
| Summary |
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 |
| Notes |
Selected conference papers |
| Bibliography |
Includes bibliographical references and index |
| Notes |
Print version record |
| In |
Springer eBooks |
| Subject |
Biophysics -- Congresses
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Bioterrorism -- Congresses
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Life sciences.
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Chemistry.
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Biological Science Disciplines
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Biotechnology
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Chemistry
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biological sciences.
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bioengineering.
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chemistry.
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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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| Genre/Form |
proceedings (reports)
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Conference papers and proceedings
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Conference papers and proceedings.
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Actes de congrès.
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| Form |
Electronic book
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| Author |
Puglisi, Joseph D.
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| LC no. |
2009926335 |
| ISBN |
9789048123681 |
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9048123682 |
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