Nuclear Magnetic Resonance, Part C

✍ Scribed by Thomas L. James, Norman J. Oppenheimer (Eds.)

• Publisher: Academic Press
• Year: 1994
• Tongue: English
• Leaves: 836
• Series: Methods in Enzymology 239
• Edition: 1
• Category: Library

✦ Synopsis

Nuclear Magnetic Resonance Spectroscopy is the only ''tool'' available for the determination of high-resolution biological molecule structure in solution. This volume includes methods for expeditiously analyzing the vast amount of data produced by the new 3D and 4D NMR techniques and for generating structures from the data and for assessing the quality of those structures. Application to various classes of important proteins and protein-ligand complexes illustrate uses of the methodology presented. Examination of techniques to explore the dynamic nature of proteins complete the volume

✦ Table of Contents

Content:
Contributors to volume 239
Pages ix-xi

Preface
Page xiii
Thomas L James, Norman J Oppenheimer

Volumes in series
Pages xv-xxix

[1] Practical introduction to theory and implementation of multinuclear, multidimensional nuclear magnetic resonance experiments Original Research Article
Pages 3-79
Arthur S. Edison, Frits Abildgaard, William M. Westler, Ed S. Mooberry, John L. Markley

[2] Measurement of homo- and heteronuclear J couplings from quantitative J correlation Original Research Article
Pages 79-105
Ad Bax, Geerten W Vuister, Stephan Grzesiek, Frank Delaglio, Andy C Wang, Rolf Tschudin, Guang Zhu

[3] Two-dimensional exchange spectroscopy of proteins Original Research Article
Pages 106-144
Slobodan Macura, William M Westler, John L Markley

[4] Pulsed-field gradients: Theory and practice Original Research Article
Pages 145-207
James Keele, Robin T Clowes, Adrian L Davis, Ernest D Laue

[5] Selective pulses and their applications to assignment and structure determination in nuclear magnetic resonance Original Research Article
Pages 207-246
Lyndon Emsley

[6] Modifications of older model nuclear magnetic resonance console for collection of multinuclear, multidimensional spectral data Original Research Article
Pages 247-256
Ed S Mooberry, Frits Abildgaard, John L Markley

[7] Using maximum likelihood spectral deconvolution in multidimensional nuclear magnetic resonance Original Research Article
Pages 257-288
Philip N Borer, George C Levy

[8] Automated and semiautomated analysis of homo- and heteronuclear multidimensional nuclear magnetic resonance spectra of proteins: The program pronto Original Research Article
Pages 288-307
Mogens Kjær, Kim Vilbour Andersen, Flemming M Poulsen

[9] Automated assignment of multidimensional nuclear magnetic resonance spectra Original Research Article
Pages 308-318
Hartmut Oschkinat, David Croft

[10] Quantitative information from complicated nuclear magnetic resonance spectra of biological macromolecules Original Research Article
Pages 318-345
Jens J Led, Henrik Gesmar

[11] Multidimensional heteronuclear nuclear magnetic resonance of proteins Original Research Article
Pages 349-363
G Marius Clore, Angela M Gronenborn

[12] Chemical shifts as a tool for structure determination Original Research Article
Pages 363-392
David S Wishart, Brian D Sykes

[13] Use of chemical shifts and coupling constants in nuclear magnetic resonance structural studies on peptides and proteins Original Research Article
Pages 392-416
David A Case, H.Jane Dyson, Peter E Wright

[14] Assessment of quality of derived macromolecular structures Original Research Article
Pages 416-439
Thomas L James

[15] Nuclear magnetic resonance study of antibodies: A multinuclear approach Original Research Article
Pages 440-464
Yoji Arata, Koichi Kato, Hideo Takahashi, Ichio Shimada

[16] Strategy for studying modular proteins: Application to complement modules Original Research Article
Pages 464-485
Paul N Barlow, Iain D Campbell

[17] Two-dimensional nuclear magnetic resonance spectra of paramagnetic systems Original Research Article
Pages 485-514
Lucia Banci, Ivano Bertini, Claudio Luchinat

[18] Methods to study membrane protein structure in solution Original Research Article
Pages 515-535
Gillian D Henry, Brian D Sykes

[19] Experimental nuclear magnetic resonance studies of membrane proteins Original Research Article
Pages 536-560
S.J Opella, Y Kim, P McDonnell

[20] Investigation of protein motions via relaxation measurements Original Research Article
Pages 563-596
Jeffrey W Peng, Gerhard Wagner

[21] Nuclear magnetic resonance measurements of slow conformational dynamics in macromolecules Original Research Article
Pages 596-619
Andrew N Lane, Jean-FranВўois LefГЁvre

[22] Accounting for molecular mobility in structure determination based on nuclear magnetic resonance spectroscopic and X-ray diffraction data Original Research Article
Pages 619-654
Wilfred F Van Gunsteren, Roger M Brunne, Piet Gros, RenГ©C Van Schaik, Celia A Schiffer, Andrew E Torda

[23] Protein-ligand interactions: Exchange processes and determination of ligand conformation and protein-ligand contacts Original Research Article
Pages 657-700
L.Y Lian, I.L Barsukov, M.J Sutcliffe, K.H Sze, G.C.K Roberts

[24] Nuclear magnetic resonance studies of protein-peptide complexes Original Research Article
Pages 700-717
A.Joshua Wand, James H Short

[25] Nuclear magnetic resonance methods for studying protein-ligand complexes Original Research Article
Pages 717-739
Andrew M Petros, Stephen W Fesik

[26] Use of nuclear magnetic resonance in probing ligand-macromolecule interactions Original Research Article
Pages 739-767
David E Wemmer, Philip G Williams

Author index
Pages 769-796

Subject index
Pages 797-813