Synopses & Reviews
This volume is a collection of articles from the proceedings of the International School of Structural Biology and Magnetic Resonance 8th Course: Biophysics and the Challenges of Emerging Threats. This NATO Advance Study Institute (ASI) was held in Erice at the Ettore Majorana Foundation and Centre for Scientific Culture on 19 through 30 June 2007. The ASI brought together a diverse group of experts who bridged the fields of virology and biology, biophysics, chemistry and physics. Prominent lecturers and students from around the world representant a total of 24 countries participated in the NATO ASI organized by Professors Joseph Puglisi (Stanford University, USA) and Alexander Arseniev (Moscow, RU). The central hypothesis underlying this ASI was that interdisciplinary research, merging principles of physics, chemistry and biology, can drive new discovery in detecting and fighting bioterrorism agents, lead to cleaner environments, and help propel development in NATO partner countries. The ASI merged the related disciplines of biophysics, biochemistry and molecular structure to treat, detect, and understand emerging infectious diseases. It addressed the treatment and detection of bioterrorism agents, and focused on critical partner country priorities in biotechnology, materials, drug discovery and the environment. It provided crossroads discussing new technologies in biophysics and structural biology, their implications pathogen detection and treatment and their role in partner country development. The ASI allowed deep and wide-ranging discussion between lecturers and students, providing overviews of key areas and links between them. The range of topics represent the diversity of critical problems between structural biology, biochemistry and biophysics, in which lies the fertile ground of drug development, biotechnology and new materials.
Synopsis
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."
Table of Contents
Preface.- List of Contributors.- A Simple Model for Protein Folding; E.R. Henry, W.A. Eaton.- Complementarity of Hydrophobic/Hydrophilic Properties in Protein Ligand Complexes: A New Tool to Improve Docking Results; T.V. Pyrkov et al.- Structures of Cvnh Family Lectins; A.M. Gronenborn.- Biohysical Approaches to Study DNA Base Flipping; S. Klimasauskas et al.- The Diversity of Nuclear Magnetic Resonance Spectroscopy; C.W. Liu.- Improved Dye Stability in Single-Molecule Fluorescence Experiments; C.E. Aitken et al.- The Evaluation of Isotope Editing and Filtering for Protein-Ligand Interaction Elucidation by NMR; I.M. Robertson et al.- Ribosome: an Ancient Cellular Nano-Machine for Genetic Code Translation; A. Yonath.- Course Abstracts and Posters.- Author Index.-