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Biological NMR Part A

Langue : Anglais

Coordonnateur : Wand A.Joshua

Couverture de l’ouvrage Biological NMR Part A

Biological NMR, Part A, the latest release in the Methods of Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters on topics such as Protein methyl labeling, Membrane protein expression ? yeast, Protein aromatic labeling, His-tag/Metal contamination, Bicelles, nanodiscs and micelles MP host, PTM ? phosphorylation, PTM ? lipidation, Screening platform for receptor-ligand discovery

Solution Spectroscopy, Large protein strategies, NUS data collection/analysis, F19 incl. hydration, ODNP - hydration, Reverse micelle - Hydration Solid State Spectroscopy, SS NMR membrane proteins, SS NMR soluble/aggregate proteins, SS DNP - general, SS NMR nucleic acids, Structure determination and computer analysis, and much more.

1. Selective Methyl Labeling of Proteins: Enabling Structural and Mechanistic Studies As Well As Drug Discovery Applications by Solution-State NMR Andrew Proudfoot, Andreas O. Frank, Alexandra Frommlet and Andreas Lingel 2. Isotopic Labeling of Eukaryotic Membrane Proteins for NMR Studies of Interactions and Dynamics Igor Dikiy, Lindsay Clark, Kevin H. Gardner and Daniel M. Rosenbaum 3. Optimal Isotope Labeling of Aromatic Amino Acid Side Chains for NMR Studies of Protein Dynamics Ulrich Weininger 4. A Quick and Colorful Method to Measure Low-Level Contaminations of Paramagnetic Ni2+ in Protein Samples Purified by Immobilized Metal Ion Affinity Chromatography Starla D. Glover and Cecilia Tommos 5. Toolkit for NMR Studies of Methyl-Labeled Proteins Paolo Rossi, Yoan R. Monneau, Youlin Xia, Yojiro Ishida and Charalampos G. Kalodimos 6. Synthetic Biology-Based Solution NMR Studies on Membrane Proteins in Lipid Environments Erik Henrich, Frank Löhr, Julija Mezhyrova, Aisha Laguerre, Frank Bernhard and Volker Dötsch 7. Preparation of Phosphorylated Proteins for NMR Spectroscopy Ganesan Senthil Kumar, Rebecca Page and Wolfgang Peti 8. Synthesis and NMR Characterization of the Prenylated Peptide, a-Factor Taysir K. Bader, Todd M. Rappe, Gianlugi Veglia and Mark D. Distefano 9. The Preparation and Solution NMR Spectroscopy of Human Glycoproteins Is Accessible and Rewarding Adam W. Barb, Daniel J. Falconer and Ganesh P. Subedi 10. Nonuniform Sampling for NMR Spectroscopy Scott Robson, Haribabu Arthanari, Sven G. Hyberts and Gerhard Wagner 11. Exploring Protein Conformational Landscapes Using High-Pressure NMR Julien Roche, Catherine A. Royer and Christian Roumestand 12. CS-ROSETTA Santrupti Nerli and Nikolaos G. Sgourakis 13. Combining Evolutionary Covariance and NMR Data for Protein Structure Determination Yuanpeng Janet Huang, Kelly P. Brock, Yojiro Ishida, Gurla V.T. Swapna, Masayori Inouye, Debora S. Marks, Chris Sander and Gaetano T. Montelione 14. Combining NMR Spectroscopy and Molecular Dynamic Simulations to Solve and Analyse the Structure of Protein–RNA Complexes Sebastien Campagne, Miroslav Krepl, Jiri Sponer and Frederic H-T. Allain

Addressed to all specialists in the field.
Dr. A. Joshua Wand teaches at the Department of Biochemistry & Biophysics, Perelman School of Medicine, University of Pennsylvania, USA
  • Provides the authority and expertise of leading contributors from an international board of authors
  • Presents the latest release in the Methods of Enzymology series
  • Updated release includes the latest information on the Biological NMR

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Ouvrage de 440 p.

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Thèmes de Biological NMR Part A :

Mots-clés :

4-(2-Pyridylazo)resorcinol; Abrelax; a-Factor; Automated NMR data analysis; AutoStructure/ASDP; Backbone assignment; Bicelles; Biomolecular NMR; Cell-free protein expression; Conformational exchange; CS-Rosetta; C-terminal ester; Data reconstruction; DFT; Drug discovery; Dynamics; Evolutionary couplings; Exhaustive search; Farnesylation; Fast NOESY data collection; FFT; Glycan remodeling; Glycoprotein expression; Glycosylhydrolase; Glycosyltransferase; GPCRs; HEK293; High pressure; Hybrid methods; IMAC; Immobilized metal ion affinity chromatography; Intermediates; Isotope labeling; Isotopic labeling; Kinase; Large proteins; Lipid bilayer; Lipidation; MAGIC algorithm; Maximum entropy; MD simulation; Membrane proteins; Methyl labeling; Model-based automatic methyl assignment; Multiple sequence alignment; Nanodiscs; N-glycoprotein; Ni2+ leakage; NMR; NMR spectroscopy; NMR structure determination; NOE assignment; Nonuniform sampling; O-glycoprotein; Order parameter; PAR; Peptide; Pheromone; Phosphatase; Phosphorylation; Pichia pastoris; Posttranslational modification; Prenylation; Protein expression; Protein families; Protein folding; Protein metal ion contaminants; Protein NMR spectroscopy; Protein–ligand interactions; Protein–RNA interactions; Purification of His-tagged proteins; RASREC; Relaxation; Resolution; Ring flips; Selective labeling; Sensitivity; Site-selective labeling; SOFAST–NOESY; Solution-state NMR; Sparse sampling; Strong couplings; Structure–function relationship; Structures; Transition state

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