NMR Spectroscopy for Probing Functional Dynamics at Biological Interfaces

Edited by Anirban Bhunia, Hanudatta S Atreya, Neeraj Sinha

Publication date:

17 August 2022

Length of book:

708 pages

Publisher

Royal Society of Chemistry

ISBN-13: 9781839165719

BOOK DESCRIPTION
TABLE OF CONTENTS

NMR spectroscopy has found a wide range of applications in life sciences over recent decades. Providing a comprehensive amalgamation of the scattered knowledge of how to apply high-resolution NMR techniques to biomolecular systems, this book will break down the conventional stereotypes in the use of NMR for structural studies. The major focus is on novel approaches in NMR which deal with the functional interface of either protein-protein interactions or protein-lipid interactions. Bridging the gaps between structural and functional studies, the Editors believe a thorough compilation of these studies will open an entirely new dimension of understanding of crucial functional motifs. This in turn will be helpful for future applications into drug design or better understanding of systems.

The book will appeal to NMR practitioners in industry and academia who are looking for a comprehensive understanding of the possibilities of applying high-resolution NMR spectroscopic techniques in probing biomolecular interactions.

Theory and Applications of NMR Spectroscopy in Bio Molecular Structures and Dynamics of Proteins; Multi-state Structures and Dynamics at Atomic Resolution Using Exact NOEs; Protein Backbone and Side-chain 15N Spin Relaxation Techniques to Study Biomacromolecular Interactions; Lineshape Analysis as a Tool for Probing Functional Motions at Biological Interfaces; Monitoring Interfaces of Thermo- and pH-responsive Polymers using Solvent Relaxation; NMR-based Ligand–Receptor Interaction Studies under Conventional and Unconventional Conditions; Multi-frequency Saturation Transfer Difference NMR to Characterize Weak Protein–Ligand Complexes; Structural Insight into the Slowly Exchanging Dark States at the Functional Interaction Interface; Dynamics of Protein–Nanoparticle Interactions Using NMR; NMR Structures, Dynamics and Interactions of Protein Complexes in B2 Integrins; Describing Dynamic Chaperone–Client Complexes by Solution NMR Spectroscopy; Methyl-TROSY NMR Spectroscopy in the Investigation of Allosteric Cooperativity in Large Biomolecular Complexes; Characterizing Conformational Diversity of G Protein-coupled receptors by Solution NMR Spectroscopy; Characterising Intrinsically Disordered Proteins using NMR Spectroscopy and Molecular Dynamics Simulations; Structure- and Dynamics-guided Drug Development Using NMR and its Application to Diverse Pharmaceutical Modalities; Locating Hydrogen Atoms Using Fast-MAS Solid-state NMR and MicroED; Membranes, Minerals and Magnets: Application of NMR Spectroscopy to Biological Interfaces; Solid-state NMR Shows that the Structure and Dynamics of Specific Residues in the Membrane Receptor CXCR1 are Altered by Interactions with Specific Residues in its Agonist IL-8; High-resolution NMR Studies of Antibiotics in Membranes; New Concepts for the Mechanisms of Action of Antimicrobial Peptides from Solid-state NMR Investigations; Structure and Dynamics of Native Biological Materials by Solid-state NMR Spectroscopy; The Lipid Phase of the Stratum Corneum Studied by Solid-state NMR: A Not So Rigid Barrier