Spectroscopy For The Biological Sciences

by Hammes, Gordon G.

• ISBN13: 9780471713449
• ISBN10: 0471713449
• Edition: 1st
• Format: Paperback
• Copyright: 2005-07-01
• Publisher: Wiley-Interscience

Summary

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'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.

Author Biography

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.

Table of Contents

PREFACE	ix
1. FUNDAMENTALS OF SPECTROSCOPY	1	(16)
Introduction	1	(2)
Quantum Mechanics	3	(2)
Particle in a Box	5	(4)
Properties of Waves	9	(4)
References	13	(1)
Problems	14	(3)
2. X-RAY CRYSTALLOGRAPHY	17	(18)
Introduction	17	(1)
Scattering of X Rays by a Crystal	18	(4)
Structure Determination	22	(3)
Neutron Diffraction	25	(1)
Nucleic Acid Structure	25	(3)
Protein Structure	28	(2)
Enzyme Catalysis	30	(2)
References	32	(1)
Problems	32	(3)
3. ELECTRONIC SPECTRA	35	(28)
Introduction	35	(1)
Absorption Spectra	36	(2)
Ultraviolet Spectra of Proteins	38	(2)
Nucleic Acid Spectra	40	(1)
Prosthetic Groups	41	(3)
Difference Spectroscopy	44	(2)
X-Ray Absorption Spectroscopy	46	(1)
Fluorescence and Phosphorescence	47	(4)
RecBCD: Helicase Activity Monitored by Fluorescence	51	(1)
Fluorescence Energy Transfer: A Molecular Ruler	52	(2)
Application of Energy Transfer to Biological Systems	54	(3)
Dihydrofolate Reductase	57	(1)
References	58	(1)
Problems	59	(4)
4. CIRCULAR DICHROISM, OPTICAL ROTARY DISPERSION, AND FLUORESCENCE POLARIZATION	63	(26)
Introduction	63	(2)
Optical Rotary Dispersion	65	(1)
Circular Dichroism	66	(1)
Optical Rotary Dispersion and Circular Dichroism of Proteins	67	(2)
Optical Rotation and Circular Dichroism of Nucleic Acids	69	(2)
Small Molecule Binding to DNA	71	(3)
Protein Folding	74	(3)
Interaction of DNA with Zinc Finger Proteins	77	(1)
Fluorescence Polarization	78	(2)
Integration of HIV Genome into Host Genome	80	(1)
α-Ketoglutarate Dehyrogenase	81	(3)
References	84	(1)
Problems	84	(5)
5. VIBRATIONS IN MACROMOLECULES	89	(14)
Introduction	89	(3)
Infrared Spectroscopy	92	(1)
Raman Spectroscopy	92	(3)
Structure Determination with Vibrational Spectroscopy	95	(3)
Resonance Raman Spectroscopy	98	(2)
Structure of Enzyme-Substrate Complexes	100	(1)
References	101	(1)
Problems	102	(1)
6. PRINCIPLES OF NUCLEAR MAGNETIC RESONANCE AND ELECTRON SPIN RESONANCE	103	(26)
Introduction	103	(3)
NMR Spectrometers	106	(2)
Chemical Shifts	108	(2)
Spin-Spin Splitting	110	(2)
Relaxation Times	112	(3)
Multidimensional NMR	115	(6)
Magnetic Resonance Imaging	121	(1)
Electron Spin Resonance	122	(3)
References	125	(1)
Problems	125	(4)
7. APPLICATIONS OF MAGNETIC RESONANCE TO BIOLOGY	129	(16)
Introduction	129	(1)
Regulation of DNA Transcription	129	(3)
Protein-DNA Interactions	132	(1)
Dynamics of Protein Folding	133	(3)
RNA Folding	136	(3)
Lactose Permease	139	(3)
Conclusion	142	(1)
References	142	(3)
8. MASS SPECTROMETRY	145	(18)
Introduction	145	(1)
Mass Analysis	145	(4)
Tandem Mass Spectrometry (MS/MS)	149	(1)
Ion Detectors	150	(1)
Ionization of the Sample	150	(4)
Sample Preparation Analysis	154	(1)
Proteins and Peptides	154	(3)
Protein Folding	157	(3)
Other Biomolecules	160	(1)
References	161	(1)
Problems	161	(2)
APPENDICES
1. Useful Constants and Conversion Factors	163	(2)
2. Structures of the Common Amino Acids at Neutral pH	165	(2)
3. Common Nucleic Acid Components	167	(2)
INDEX	169