This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications. The book, in honor of Oleg Jardetsky, one of the pioneers of the field, is edited by two of the most highly respected investigators using NMR, and features contributions by most of the leading workers in the field. It will be valued as a landmark publication that presents the state-of-the-art perspectives regarding one of today's most important technologies.…mehr
This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications. The book, in honor of Oleg Jardetsky, one of the pioneers of the field, is edited by two of the most highly respected investigators using NMR, and features contributions by most of the leading workers in the field. It will be valued as a landmark publication that presents the state-of-the-art perspectives regarding one of today's most important technologies.Hinweis: Dieser Artikel kann nur an eine deutsche Lieferadresse ausgeliefert werden.
* SECTION I: History of the Biological NMR Spectroscopy * 1: O. Jardetsky: Simple Insights from the Beginnings of Magnetic Resonance in Molecular Biology * 2: M. Cohn: Choice of Problems in the Early Days of Biochemical NMR * 3: R.G. Shulman: Early Days of Biochemical NMR * 4: J.J.H. Ackerman: William D. Phillips Memorial Lecture * SECTION II: Protein Structural Studies * 5: M.R. Gryk and O. Jardetsky: Flexibility and Function of the Escherichia coli trp Repressor * 6: M.J. Revington W. Lee and C.H. Arrowsmith: Heteronuclear Strategies for the Assignment of Larger Protein/DNA Complexes * 7: C. Ho and H.-W. Kim: Design of Novel Hemoglobins * 8: C.M. Dobson: The Role of NMR Spectroscopy in Understanding how Proteins Fold * 9: G.C.K. Roberts L.-Y. Lian I.L. Barsukov S. Modi and W.U. Primrose: NMR Approaches to Understanding Protein Specificity * 10: A.P. Hinck W.F. Walkenhorst D.M. Truckses and J.L. Markley: NMR and Mutagenesis Investigations of a Model Cis:Trans Peptide Isomerization Reaction * 11: S.J.Opella L.E. Chirlian and B. Bechinger: A Solid State NMR Approach to Structure Determination of Membrane Associated Peptides and Proteins * 12: K. Akasaka T Yamaguchi H. Yamada Y. Kamatari and T. Konno: NMR Approach to the Heat- Cold- and pressure-Induced Unfolding of Proteins * 13: F. Mari X. Xie J.H. Simpson and D.J. Nelson: Multidimensional NMR Investigation of the Neurotoxic Peptide mastoparan in the Absence and Presence of Calmodulin * 14: Y. Arata: NMR of Larger Proteins * 15: K.S. Matthews: Selective Chemical Deuteration of Aromatic Amino Acids * 16: T. Jardetsky: The Interactions of Antigens and Superantigens with the Human Class II Major Histocompatibility complex Molecule HLA-DR1 * 17: W.N. Lipscomb: Chorismate Mutase Essentially a Template Enzyme * SECTION III: Nucleic Acids * 18: R. Chen D. Fink and R.B. Altman: Computing the Structure of Large Complexes * 19: D. Wemmer: Design and Characterization of New Sequence Specific DNA Ligands * 20: C. Milhe A. Lane and J.F. Lefévre: Determination by 1H NMR of a Slow Conformational Transition and Hydration Change in the Consensus TATAAT Pribnow Box * SECTION IV: In Vivo Spectroscopy * 21: P.J. Cozzone J. Vion-Dury S. Confort-Gouny F. Nicoli A.-M. Salvan and S. Lamoreux: Clinicians Need Localized Proton MRS of the Brain in the Management of HIV-related Encephalopathies * 22: O. Kaplan and J.S. Cohen: Nuclear Magnetic Resonance Spectroscopy Studies of cancer Cell Metabolism * 23: L. Litt M.T. espanol Y. Xu Y. Cohen L.-H. chang P.R. Weinstein P.H. Chan and T.L. James: Ex Vivo Multinuclear NMR Spectroscopy of Perfused respiring Rat Brain Slices
* SECTION I: History of the Biological NMR Spectroscopy * 1: O. Jardetsky: Simple Insights from the Beginnings of Magnetic Resonance in Molecular Biology * 2: M. Cohn: Choice of Problems in the Early Days of Biochemical NMR * 3: R.G. Shulman: Early Days of Biochemical NMR * 4: J.J.H. Ackerman: William D. Phillips Memorial Lecture * SECTION II: Protein Structural Studies * 5: M.R. Gryk and O. Jardetsky: Flexibility and Function of the Escherichia coli trp Repressor * 6: M.J. Revington W. Lee and C.H. Arrowsmith: Heteronuclear Strategies for the Assignment of Larger Protein/DNA Complexes * 7: C. Ho and H.-W. Kim: Design of Novel Hemoglobins * 8: C.M. Dobson: The Role of NMR Spectroscopy in Understanding how Proteins Fold * 9: G.C.K. Roberts L.-Y. Lian I.L. Barsukov S. Modi and W.U. Primrose: NMR Approaches to Understanding Protein Specificity * 10: A.P. Hinck W.F. Walkenhorst D.M. Truckses and J.L. Markley: NMR and Mutagenesis Investigations of a Model Cis:Trans Peptide Isomerization Reaction * 11: S.J.Opella L.E. Chirlian and B. Bechinger: A Solid State NMR Approach to Structure Determination of Membrane Associated Peptides and Proteins * 12: K. Akasaka T Yamaguchi H. Yamada Y. Kamatari and T. Konno: NMR Approach to the Heat- Cold- and pressure-Induced Unfolding of Proteins * 13: F. Mari X. Xie J.H. Simpson and D.J. Nelson: Multidimensional NMR Investigation of the Neurotoxic Peptide mastoparan in the Absence and Presence of Calmodulin * 14: Y. Arata: NMR of Larger Proteins * 15: K.S. Matthews: Selective Chemical Deuteration of Aromatic Amino Acids * 16: T. Jardetsky: The Interactions of Antigens and Superantigens with the Human Class II Major Histocompatibility complex Molecule HLA-DR1 * 17: W.N. Lipscomb: Chorismate Mutase Essentially a Template Enzyme * SECTION III: Nucleic Acids * 18: R. Chen D. Fink and R.B. Altman: Computing the Structure of Large Complexes * 19: D. Wemmer: Design and Characterization of New Sequence Specific DNA Ligands * 20: C. Milhe A. Lane and J.F. Lefévre: Determination by 1H NMR of a Slow Conformational Transition and Hydration Change in the Consensus TATAAT Pribnow Box * SECTION IV: In Vivo Spectroscopy * 21: P.J. Cozzone J. Vion-Dury S. Confort-Gouny F. Nicoli A.-M. Salvan and S. Lamoreux: Clinicians Need Localized Proton MRS of the Brain in the Management of HIV-related Encephalopathies * 22: O. Kaplan and J.S. Cohen: Nuclear Magnetic Resonance Spectroscopy Studies of cancer Cell Metabolism * 23: L. Litt M.T. espanol Y. Xu Y. Cohen L.-H. chang P.R. Weinstein P.H. Chan and T.L. James: Ex Vivo Multinuclear NMR Spectroscopy of Perfused respiring Rat Brain Slices
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