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′s 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.)
- 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.
1. FUNDAMENTALS OF SPECTROSCOPY.
Particle in a Box.
Properties of Waves.
2. X–RAY CRYSTALLOGRAPHY.
Scattering of X Rays by a Crystal.
Nucleic Acid Structure.
3. ELECTRONIC SPECTRA.
Ultraviolet Spectra of Proteins.
Nucleic Acid Spectra.
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 .
4. CIRCULAR DICHROISM, OPTICAL ROTARY DISPERSION, AND FLUORESCENCE POLARIZATION.
Optical Rotary Dispersion.
Optical Rotary Dispersion and Circular Dichroism of Proteins.
Optical Rotation and Circular Dichroism of Nucleic Acids.
Small Molecule Binding to DNA.
Interaction of DNA with Zinc Finger Proteins.
Integration of HIV Genome into Host Genome.
5. VIBRATIONS IN MACROMOLECULES.
Structure Determination with Vibrational Spectroscopy Resonance Raman Spectroscopy.
Structure of Enzyme–Substrate Complexes.
6. PRINCIPLES OF NUCLEAR MAGNETIC RESONANCE AND ELECTRON SPIN RESONANCE.
Magnetic Resonance Imaging.
Electron Spin Resonance.
7. APPLICATIONS OF MAGNETIC RESONANCE TO BIOLOGY.
Regulation of DNA Transcription.
Dynamics of Protein Folding.
8. MASS SPECTROMETRY.
Tandem Mass Spectrometry (MS/MS)..
Ionization of the Sample.
Proteins and Peptides.
1. Useful Constants and Conversion Factors.
2. Structures of the Common Amino Acids at Neutral pH.
3. Common Nucleic Acid Components.