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Rupp, B. Garland Pub. 2009.10 * Synthesizing over thirty years of advances into a comprehensive textbook, Biomolecular Crystallography describes the fundamentals, practices, and applications of protein crystallography. Deftly illustrated in full-color by the author, the text describes mathematical and physical concepts in accessible and accurate language. It distills key concepts for understanding the practice and analysis of protein crystal structures and contains examples of biologically-relevant molecules, complexes, and drug target structures. * Harris, R. K. et al. ed. John Wiley & Sons 2010.1 * Indeed, NMR can now be used to refine diffraction results and, in favorable cases, to solve crystal structures with minimal (or even no) diffraction data. The increasing ability to relate chemical shifts (including the tensor components) to the crystallographic location of relevant atoms in the unit cell via computational methods has added significantly to the practice of NMR crystallography. Diffraction experts will increasingly welcome NMR as an allied technique in their structural analyses. Indeed, it may be that in the future crystal structures will be determined by simultaneously fitting diffraction patterns and NMR spectra. * This Handbook is organised into six sections. The first contains an overview and some articles on fundamental NMR topics, followed by a section concentrating on chemical shifts, and one on coupling interactions. The fourth section contains articles describing how NMR results relate to fundamental crystallography concepts and to diffraction methods. The fifth section concerns specific aspects of structure, such as hydrogen bonding. Finally, four articles in the sixth section give applications of NMR crystallography to structural biology, organic & pharmaceutical chemistry, inorganic & materials chemistry, and geochemistry. * Hinterdorfer, P. & van Oijen, A. ed. Springer-Verlag 2009.7 1. Single-molecule fluorescence tracking/ 2. Single molecule studies in the membrane/ 3. Single-molecule imaging in live cells/ 4. Superresolution imaging/ 5. Fluorescence Resonance Energy Transfer/ 6. Single-molecule enzymology/ 7. Rotary proteins/ 8. Fluorescence Correlation Spectroscopy/ 9. Advanced Concepts of Fluorescence Fluctuation Spectroscopy/ 10. Nucleic-acid analysis at the single-molecule level/ 11. Nanopores: Geneneration and Single-Molecule Applications/ 12. Optical trapping/ 13. Magnetic tweezing/ 14. Protein/DNA unfolding/ 15. Single molecule recognition/ 16. Nano-scale AFM imaging/ 17. High Speed AFM/ 18. Recognition imaging/ 19. Atomic force microscopy of protein-protein interactions/ 20. A New Approach to Analysis of Single Molecule Force Measurements/ 21. Single Molecule Recognition: Extracting Information from Individual Binding Events and Their Correlation/ Index/ * He, B. B. John Wiley & Sons 2009.8 * Experimental examples in materials research, pharmaceuticals, and forensics are also given. This presents a key resource to researchers in materials science, chemistry, physics, and pharmaceuticals, as well as graduate-level students in these areas. * Leubner, I. CRC Press 2009.9 * At the cutting edge of crystallization science and technology, this volume presents information never before available. Introducing the Balanced Nucleation and Growth (BNG) model, the book demonstrates how the results of the nucleation process are quantitatively related to practical experimental control values such as: ・reaction addition rate ・crystal solubility ・temperature ・residence time (continuous crystallizations) ・the effect of ripening agents (crystal supersizing) during nucleation ・the effect of crystal growth restrainers (crystal nanosizing) during nucleation ・control of renucleation * Waigh, T. John Wiley & Sons 2007.9 Walker, J. M. ed. Humana Press 2009.11 * Since the publication of the bestselling second edition of John Walker's widely acclaimed Protein Protocols Handbook, there have been continual methodological developments in the field of protein chemistry. This greatly enhanced third edition introduces 57 critically important new chapters, as well as significantly updating the previous edition's tried-and-true methods. Although the timely new chapters are spread throughout all of the book, the vital sectionハon post-translational modifications has been expanded most to reflect the increasing importance of these modifications inハthe understanding of protein function. * |
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