Keywords:
Nuclear magnetic resonance spectroscopy.
;
Molecular biology -- Technique.
;
Biochemistry -- Technique.
;
Electronic books.
Description / Table of Contents:
NMR in Molecular Biology provides an introduction to the basic concepts and principles of nuclear magnetic resonance (NMR) that are essential to a critical evaluation of experimental data. It also aims to acquaint readers in some detail with those prototype experiments in which a definite, biologically relevant answer has been obtained. The book opens with a chapter on the historical development of NMR technology. Separate chapters follow on the fundamental principles of NMR; paramagnetic perturbations of NMR spectra; time scales, chemical exchange, and problems of exchange; and characteristics of NMR spectra through investigations of compounds such as amino acids and peptides; and nucleic acid bases, nucleosides, and nucleotides. Subsequent chapters deal with protein NRM spectra, protein-ligand interactions, and the structure and dynamics of membranes. This book is intended for the student or practicing scientist wishing to gain a critical understanding of the applications of NMR to a wide range of problems in molecular biology.
Type of Medium:
Online Resource
Pages:
1 online resource (698 pages)
Edition:
1st ed.
ISBN:
9781483281858
URL:
https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=1820036
DDC:
574.19285
Language:
English
Note:
Front Cover -- NMR in Molecular Biology -- Copyright Page -- Table of Contents -- Preface -- Acknowledgments -- Chapter I. Introduction Text -- Chapter II. Fundamental Principles -- A. The NMR Phenomenon -- B. The NMR Experiment -- C. NMR on a Population of Identical Nuclei -- D. The Chemical Shift -- E. Spin-Spin Coupling -- F. Fourier Transform NMR Spectroscopy -- G. Microscopic Theory of Relaxation -- H. Relaxation in Multispin Systems -- Chapter III. Paramagnetic Perturbations of NMR Spectra -- A. General Comments -- B. General Theory of Paramagnetic Perturbations -- C. Paramagnetic Shifts and Relaxation in Metalloproteins -- D. The Extrinsic Paramagnetic Probe Method -- E. Chemically and Photochemically Induced Dynamic Nuclear Polarization (CIDNP and Photo-CIDNP) -- Chapter IV. Time-Dependent Phenomena and Problems of Averaging -- A. Definition of Time Scales -- B. Chemical Exchange -- C. Problems of Fast Exchange -- Chapter V. Amino Acids and Peptides -- A. Amino Acids -- B. Peptides -- C. Polyamino Acids and the Helix-Coil Transition -- D. Conclusion -- Chapter VI. Nucleic Acid Bases, Nucleosides, and Nucleotides -- A. Tautomerism and Ionization -- B. Molecular Interactions -- C. Nucleoside and Mononucleotide Conformation -- D. Dinucleotide Conformation -- E. Conclusion -- Chapter VII. Introduction to Protein NMR Spectra: General Features and Methodology -- A. The 1H Spectrum -- B. The 13C Spectrum -- C. Secondary and Tertiary Structure Shifts -- D. Experimental Limitations -- E. Methods for Improving Resolution -- F. Strategies for Assignment -- Chapter VIII. Solution Structure and Conformational Transitions in Proteins -- A. Comparisons of Solution and Crystal Structure -- B. Detection of Specific Structural Features -- C. Detection of Conformational Change -- D. Protein Folding -- Chapter IX. Protein-Ligand Interactions Part I.
,
A. General Considerations -- B. Ribonuclease -- C. Staphylococcal Nuclease -- D. Lysozyme -- E. Dihydrofolate Reductase -- F. Antibody-Combining Sites -- G. Alkaline Phosphatase -- H. Gene 5 Protein -- Chapter X. Protein-Ligand Interactions Part II -- A. Kinases (Phosphotransferases) -- B. Dehydrogenases -- C. Serine Proteases -- D. Aspartate Transcarbamylase -- E. Glycogen Phosphorylase -- F. Concanavalin A -- G. Aspartate Aminotransferase -- H. Glutamine Synthetase -- I. Protein Hydration and Ion Binding -- Chapter XI. Enzyme Mechanisms -- A. Structural Considerations -- B. Substrate Equilibria -- C. Stereochemistry and Isotope Exchange -- D. Observation of Intermediates and Intermediate Analogs -- E. Studies of the Catalytic Process -- Chapter XII. Protein Dynamics -- A. General Considerations -- B. Qualitative Evidence for the Flexibility of Protein Segments and Domains -- C. Quantitative Study of Internal Motions by Relaxation Methods -- Chapter XIII. Nucleic Acids and Nucleic Acid-Protein Interactions -- A. Types of Problems Investigated -- B. Oligo- and Polynucleotides -- C. Transfer RNA -- D. DNA -- E. Binding and Intercalation -- F. Nucleic Acid-Protein Interactions -- Chapter XIV. Structure and Dynamics of Membranes -- A. Organization and Mobility of Hydrocarbon Chains in Phospholipid Structures -- B. Conformational Studies on Phospholipid Head Groups -- C. EflFects of Cholesterol and Other Molecules Dissolved in the Bilayer -- D. Hydration and Ion Binding -- E. Ionophores in Phospholipid Bilayers -- F. Protein-Lipid Interactions -- G. Studies of Natural Membranes -- Appendix I. Definition of Symbols -- Appendix II. Vector, Tensor, and Matrix Notation -- References -- Author Index -- Subject Index.
Permalink