This is an introduction to the physical principles of spectroscopy and their applications to the biological sciences. Advances in such fields as proteomics and genomics place new demands on students and professionals to be able to apply quantitative concepts to the biological phenomena that they are studying. "Spectroscopy for the Biological Sciences" provides students and professionals with a working knowledge of the physical chemical aspects of spectroscopy, along with their applications to important biological problems. Designed as a companion to Professor Hammes' "Thermodynamics and Kinetics for the Biological Sciences", this approachable yet thorough text covers the basic principles of spectroscopy, including: fundamentals of spectroscopy, Electronic spectra, Circular dichroism and optical rotary dispersion, Vibration in macromolecules (IR, Raman, etc.); and Magnetic resonance, X-ray crystallography, Mass spectrometry. With a minimum of mathematics and a strong focus on applications to biology, this book will prepare current and future professionals to better understand the quantitative interpretation of biological phenomena and to utilize these tools in their work.
Rezensionen / Stimmen
"...everything about this book seems to be right...If you are a student or researcher in the biological sciences who needs a brief refresher in biological spectroscopy, this is the book you must read." (Biochemistry and Molecular Biology Education, March/April 2006) "...a valuable overview of the spectroscopy techniques commonly encountered in biological research..." (The Quarterly Review of Biology, March 2006) "...a great introduction to the world of spectroscopic methods." (Applied Spectroscopy, October 2005)
Sprache
Verlagsort
Verlagsgruppe
Zielgruppe
Für höhere Schule und Studium
Für Beruf und Forschung
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ISBN-13
978-0-471-73355-3 (9780471733553)
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Schweitzer Klassifikation
GORDON G. HAMMES is University Distinguished Service Professor of Biochemistry at Duke University Medical Center in Durham, North Carolina. He is author of Thermodynamics and Kinetics for the Biological Sciences (also from Wiley) and more than 200 research articles.
PREFACE. 1. FUNDAMENTALS OF SPECTROSCOPY. Introduction. Quantum Mechanics. Particle in a Box. Properties of Waves. References. Problems. 2. X--RAY CRYSTALLOGRAPHY. Introduction. Scattering of X Rays by a Crystal. Structure Determination. Neutron Diffraction. Nucleic Acid Structure. Protein Structure. Enzyme Catalysis. References. Problems. 3. ELECTRONIC SPECTRA. Introduction. Absorption Spectra. Ultraviolet Spectra of Proteins. Nucleic Acid Spectra. Prosthetic Groups. Difference Spectroscopy. X--Ray Absorption Spectroscopy. Fluorescence and Phosphorescence. RecBCD: Helicase Activity Monitored by Fluorescence. Fluorescence Energy Transfer: A Molecular Ruler. Application of Energy Transfer to Biological Systems. Dihydrofolate Reductase . References . Problems. 4. CIRCULAR DICHROISM, OPTICAL ROTARY DISPERSION, AND FLUORESCENCE POLARIZATION. Introduction. Optical Rotary Dispersion. Circular Dichroism. Optical Rotary Dispersion and Circular Dichroism of Proteins. Optical Rotation and Circular Dichroism of Nucleic Acids. Small Molecule Binding to DNA. Protein Folding. Interaction of DNA with Zinc Finger Proteins. Fluorescence Polarization. Integration of HIV Genome into Host Genome. alpha--Ketoglutarate Dehyrogenase. References. Problems. 5. VIBRATIONS IN MACROMOLECULES. Introduction. Infrared Spectroscopy. Raman Spectroscopy. Structure Determination with Vibrational Spectroscopy Resonance Raman Spectroscopy. Structure of Enzyme--Substrate Complexes. References. Problems. 6. PRINCIPLES OF NUCLEAR MAGNETIC RESONANCE AND ELECTRON SPIN RESONANCE. Introduction. NMR Spectrometers. Chemical Shifts. Spin--Spin Splitting. Relaxation Times. Multidimensional NMR. Magnetic Resonance Imaging. Electron Spin Resonance. References. Problems. 7. APPLICATIONS OF MAGNETIC RESONANCE TO BIOLOGY. Introduction. Regulation of DNA Transcription. Protein--DNA Interactions. Dynamics of Protein Folding. RNA Folding. Lactose Permease. Conclusion. References. 8. MASS SPECTROMETRY. Introduction. Mass Analysis. Tandem Mass Spectrometry (MS/MS).. Ion Detectors. Ionization of the Sample. Sample Preparation/Analysis. Proteins and Peptides. Protein Folding. Other Biomolecules. References. Problems. APPENDICES. 1. Useful Constants and Conversion Factors. 2. Structures of the Common Amino Acids at Neutral pH. 3. Common Nucleic Acid Components. INDEX.
