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were impossible to study as recently as ten years ago. This third edition of Protein NMR Techniques, expands upon the previous editions with;
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a wide range of applications in life sciences over recent decades. This up-to-date volume covers NMR techniques and their application to;
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High-Resolution NMR Techniques in Organic Chemistry, Third Edition describes the most important NMR spectroscopy techniques for the;
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Protein NMR Spectroscopy, Second Edition combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive;
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Techniques in Protein Chemistry VII, a valuable bench-top reference tool for protein chemists, features the most up-to-date advances;
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transform techniques and the techniques of biotech- nology. Now it is possible, with small proteins up to 10,000-12,000 daltons, by 2D FT NMR;
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This book covers new techniques in protein NMR, from basic principles to state-of-the-art research. It covers a spectrum of topics ranging;
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in Studying Proteins by NMR, by Kang Chen und Nico Tjandra NMR Studies of Metalloproteins, by Hongyan Li and Hongzhe Sun Recent Developments;
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- hydration, Reverse micelle - Hydration, Solid State Spectroscopy, SS NMR membrane proteins, SS NMR soluble/aggregate proteins, SS DNP - general, SS;
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- hydration, Reverse micelle - Hydration Solid State Spectroscopy, SS NMR membrane proteins, SS NMR soluble/aggregate proteins, SS DNP - general, SS;
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This volume covers state-of-the-art applications of solid-state and solution nuclear magnetic resonance( NMR) spectroscopy to study protein;
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degradation, along with a myriad of spectroscopic techniques that can be used to elucidate protein structure: NMR and EPR spectroscopies, FTIR;
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Nuclear magnetic resonance (NMR) is an analytical tool used by chemists and physicists to study the structure and dynamics of molecules;
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Nuclear magnetic resonance (NMR) is an analytical tool used by chemists and physicists to study the structure and dynamics of molecules;
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trap; structure-function correlation study using optical biosensors of microcolorimetrical techniques; structural proteomics as NMR or;
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describes two key nuclear magnetic resonance (NMR) methods for the investigation of protein-protein interactions, chemical shift perturbation, and;
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NMR spectroscopy is widely used in biomolecular science particularly for structure determination of proteins, nucleic acids and;
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not limited to ITC, SPR, and both ligand-detected and protein-detected NMR. Topics covered include: Design considerations in biophysical;
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proteins studied in parallel. It gives a modest overview of existing and proven techniques as well as a detailed examination of less established;
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proteins studied in parallel. It gives a modest overview of existing and proven techniques as well as a detailed examination of less established;
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expression and biophysical techniques such as fluorescence spectroscopy, NMR, mass spectrometry, cryo-electron microscopy, and X-ray crystallography;
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invaluable guide to the principal techniques used to study the interactions of proteins and ligands. This second volume covers the major;
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In this volume, a detailed description of cutting-edge computational methods applied to protein modeling as well as specific applications;
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This work elucidates the power of modern nuclear magnetic resonance (NMR) techniques to solve a wide range of practical problems that arise;
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covers, in detail, the technical and biophysical aspects of in vivo NMR techniques and includes novel developments in the field such as;
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following techniques are covered in detail: - Purification and determination of proteins - Measuring enzymatic activity - Microcalorimetry;
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become familiar with new techniques and applications in NMR spectroscopy. Chapters in this new release cover In Operando NMR Studies, Recent;
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