عنوان

Biophysics and the challenges of emerging threats /

9048123682

9789048123681

9048123666

9048123674

9789048123667

9789048123674

b710296

Biophysics and the challenges of emerging threats /

[Book]

edited by Joseph D. Puglisi.

Dordrecht :

Springer,

©2009.

1 online resource (vii, 179 pages) :

illustrations

NATO science for peace and security series. Series B, physics and biophysics

Selected conference papers.

Includes bibliographical references and index.

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.

0

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.

Springer

978-90-481-2367-4

Biophysics and the challenges of emerging threats.

9048123666

Biophysics, Congresses.

Bioterrorism, Congresses.

Biophysics.

Biophysics.

Bioterrorism.

Bioterrorism.

Physique.

PSA.

SCI086000.

Puglisi, Joseph D.

NATO Advanced Study Institute on Biophysics and the Challenges of Emerging Threats(2007 :, Erice, Italy)

20201208010311.0

pn

[Book]

Y