Download or read book Structural Studies of Membrane associated Complexes by Solid state NMR written by and published by . This book was released on 2014 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Solid state NMR written by Frances Separovic and published by . This book was released on 2020 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: The purpose of this book is to describe the methodology and applications of solid-state NMR spectroscopy to studies of membrane proteins, membrane-active peptides and model biological membranes. As well as structural studies, this book contains coverage of membrane interactions and molecular motions. Advances in biological solid-state NMR are very pertinent with high-field developments seeing applications in biological membranes and whole cells. Experts who are leaders in the development and application of biological solid-state NMR are chapter contributors. Part of Biophysical Society-IOP series.
Download or read book Solid state NMR Studies of Membrane Proteins and Membrane Protein Complexes written by Lindsay J. Sperling and published by . This book was released on 2011 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: Membrane proteins help control nearly every process in the cell, which is why approximately 50% of pharmaceuticals currently on the market target membrane proteins. Knowledge of structure-function relationships of these proteins could be leveraged to produce more efficient drugs. However, the traits that make membrane proteins so interesting also make them difficult targets for traditional structure elucidation techniques. X-ray crystallography relies on the use of single crystals, production of which are elusive for membrane proteins due to their inherent dynamic loops and stretches of hydrophobic residues, which contribute to aggregation and/or loss of function without the presence of a lipid environment. Solution NMR experiences difficulty dealing with slow molecular tumbling due to the large sizes of membrane proteins. Conversely, solid-state NMR (SSNMR) has no inherent size limitation and does not require the use of crystals, which presents SSNMR with the unique capability to study membrane proteins in native environments at atomic-resolution. However, this technique is still a relatively new tool for solving structures of biomolecules. Here, we begin to develop strategies for solid-state NMR de novo structure determination. We provide a 0́−divide-and-conquer0́+ investigation of an E. coli 41 kDa membrane protein complex, DsbA/DsbB. We begin by completing chemical shift assignments, the first step in structure determination in NMR studies, of the 21 kDa protein DsbA to optimize sensitivity and resolution of data collection and analysis of large systems. We then use this study to drive forward structural examination of the disulfide bond forming system DsbA/DsbB. Finally, SSNMR techniques are used to study a 144 kDa cytochrome bo3 ubiquinol oxidase demonstrating the power of this technique to investigate large membrane complexes in native environments.
Download or read book Perspectives on Solid State NMR in Biology written by S.R. Kiihne and published by Springer Science & Business Media. This book was released on 2013-03-14 with total page 227 pages. Available in PDF, EPUB and Kindle. Book excerpt: Solid state NMR is rapidly emerging as a universally applicable method for the characterization of ordered structures that cannot be studied with solution methods or diffraction techniques. This proceedings -; from a recent international workshop - captures an image of the latest developments and future directions for solid state NMR in biological research, particularly on membrane proteins. Detailed information on how hormones or drugs bind to their membrane receptor targets is needed, e.g. for rational drug design. Higher fields are bringing clear improvements, and the power of solid state NMR techniques for studying amorphous and membrane associated peptides, proteins and complexes is shown by examples of applications at ultra-high fields. Progress in protein expression, experimental design and data analysis are also presented by leaders in these research areas.
Download or read book Advances in Biological Solid State NMR written by Frances Separovic and published by Royal Society of Chemistry. This book was released on 2014 with total page 632 pages. Available in PDF, EPUB and Kindle. Book excerpt: Advances in Biological NMR brings the reader up to date with chapters from international leaders of this growing field, covering the most recent developments in the methodology and applications of solid state NMR to studies of membrane interactions and molecular motions
Download or read book NMR of Proteins written by Clore and published by CRC Press. This book was released on 1993 with total page 328 pages. Available in PDF, EPUB and Kindle. Book excerpt: Determination of structures of larger proteins in solution by three- and four-dimensional heteronuclear magnetic resonance spectroscopy. Methodological advances in protein NMR. Determination of high-resolution NMR structures of proteins. Multidimensional NMR studies of immunosuppressant/immunophilin complexes. NMR studies of the structure and role of modules involved in protein-protein interactions. NMR structural studies of membrane proteins. Heteronuclear NMR studies of the molecular synamics of staphylococcal nuclease. Study of protein dynamics by NMR. The folding, stability and dynamics of T4 lysozyme: a perspective using nuclear magnetic resonance.
Download or read book Membrane Protein Structure Determination written by Jean-Jacques Lacapère and published by Methods in Molecular Biology. This book was released on 2010-08-06 with total page 482 pages. Available in PDF, EPUB and Kindle. Book excerpt: Membrane proteins, representing nearly 40% of all proteins, are key components of cells involved in many cellular processes, yet only a small number of their structures have been determined. Membrane Protein Structure Determination: Methods and Protocols presents many detailed techniques for membrane protein structure determination used today by bringing together contributions from top experts in the field. Divided into five convenient sections, the book covers various strategies to purify membrane proteins, approaches to get three dimensional crystals and solve the structure by x-ray diffraction, possibilities to gain structural information for a membrane protein using electron microscopy observations, recent advances in nuclear magnetic resonance (NMR), and molecular modelling strategies that can be used either to get membrane protein structures or to move from atomic structure to a dynamic understanding of a molecular functioning mechanism. Written in the highly successful Methods in Molecular BiologyTM series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Comprehensive and easy to use, Membrane Protein Structure Determination: Methods and Protocols serves as an ideal reference for scientists seeking to further our knowledge of these vital and versatile proteins as well as our overall understanding of the complicated world of cell biology.
Download or read book Advances in Biological Solid State NMR written by Frances Separovic and published by Royal Society of Chemistry. This book was released on 2014-03-17 with total page 632 pages. Available in PDF, EPUB and Kindle. Book excerpt: The complexity and heterogeneity of biological systems has posed an immense challenge in recent years. An increasingly important tool for obtaining molecular and atomic scale information on a range of large biological molecules and cellular components is solid-state NMR. This technique can address fascinating problems in structural biology, including the arrangement of supramolecular complexes and fibril formation in relation to molecular folding, misfolding and aggregation. Advances in Biological Solid-State NMR brings the reader up to date with chapters from international leaders of this growing field, covering the most recent developments in the methodology and applications of solid-state NMR to studies of membrane interactions and molecular motions. A much needed discussion of membrane systems is detailed alongside important developments in in situ analysis. Topics include applications to biological membranes, membrane active peptides, membrane proteins, protein assemblies and in-cell NMR. This exposition of an invaluable technique will interest those working in a range of related spectroscopic and biological fields. A basic introduction invites those interested to familiarise themselves with the basic mathematical and conceptual foundations of solid-state NMR. A thorough and comprehensive discussion of this promising technique follows, which is essential reading for those working or studying at postgraduate level in this exciting field.
Download or read book Dynamic and Structural Studies of Membrane Proteins by Oriented Sample Solid State NMR written by Emmanuel Oluwaseyi Awosanya and published by . This book was released on 2020 with total page 97 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book High Resolution Structural Studies of Membrane Proteins Using Solid State NMR written by Lubica Aslimovska and published by . This book was released on 2007 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Experimental Approaches of NMR Spectroscopy written by The Nuclear Magnetic Resonance Society of Japan and published by Springer. This book was released on 2017-11-23 with total page 634 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book describes the advanced developments in methodology and applications of NMR spectroscopy to life science and materials science. Experts who are leaders in the development of new methods and applications of life and material sciences have contributed an exciting range of topics that cover recent advances in structural determination of biological and material molecules, dynamic aspects of biological and material molecules, and development of novel NMR techniques, including resolution and sensitivity enhancement. First, this book particularly emphasizes the experimental details for new researchers to use NMR spectroscopy and pick up the potentials of NMR spectroscopy. Second, the book is designed for those who are involved in either developing the technique or expanding the NMR application fields by applying them to specific samples. Third, the Nuclear Magnetic Resonance Society of Japan has organized this book not only for NMR members of Japan but also for readers worldwide who are interested in using NMR spectroscopy extensively.
Download or read book Nmr In Structural Biology A Collection Of Papers By Kurt Wuthrich written by Kurt Wuthrich and published by World Scientific. This book was released on 1995-07-31 with total page 760 pages. Available in PDF, EPUB and Kindle. Book excerpt: The volume presents a survey of the research by Kurt Wüthrich and his associates during the period 1965 to 1994. A selection of reprints of original papers on the use of NMR spectroscopy in structural biology is supplemented with an introduction, which outlines the foundations and the historical development of the use of NMR spectroscopy for the determination of three-dimensional structures of biological macromolecules in solution. The original papers are presented in groups highlighting protein structure determination by NMR, studies of dynamic properties and hydration of biological macromolecules, and practical applications of the NMR methodology in fields such as enzymology, transcriptional regulation, immunosuppression and protein folding.
Download or read book NMR of Proteins and Small Biomolecules written by Guang Zhu and published by Springer Science & Business Media. This book was released on 2012-03-28 with total page 255 pages. Available in PDF, EPUB and Kindle. Book excerpt: Application of NMR and Molecular Docking in Structure-Based Drug Discovery, by Jaime L. Stark and Robert Powers NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions, by Olga Vinogradova and Jun Qin The Use of Residual Dipolar Coupling in Studying Proteins by NMR, by Kang Chen und Nico Tjandra NMR Studies of Metalloproteins, by Hongyan Li and Hongzhe Sun Recent Developments in 15N NMR Relaxation Studies that Probe Protein Backbone Dynamics, by Rieko Ishima Contemporary Methods in Structure Determination of Membrane Proteins by Solution NMR, by Tabussom Qureshi and Natalie K. Goto Protein Structure Determination by Solid-State NMR, by Xin Zhao Dynamic Nuclear Polarization: New Methodology and Applications, by Kong Hung Sze, Qinglin Wu, Ho Sum Tse and Guang Zhu
Download or read book Structure and Dynamics of Membrane Proteins from Solid state NMR written by Myungwoon Lee and published by . This book was released on 2018 with total page 241 pages. Available in PDF, EPUB and Kindle. Book excerpt: Solid-state nuclear magnetic resonance (SSNMR) spectroscopy is an essential tool to elucidate the structure, dynamics, and function of biomolecules. This thesis mainly focuses on the structure determination of the hydrophobic domains for fusion proteins which are involved in membrane fusion between the cell membrane and viral envelope. Although extensive structural studies have been conducted on the soluble ectodomain by crystallography, the structural topologies of the hydrophobic TMD of the fusion proteins have been poorly understood. Here, we introduced SSNMR to investigate the secondary structure and oligomeric states of the TMD of two fusion proteins, PIV5 F and HIV gp41. For the PIV5 TMD, the membrane dependent secondary structure was determined by measuring the chemical shifts: predominant a-helical conformation in the POPC/cholesterol membrane shifts to the [Beta]-strand in the POPE membrane. Using 19F spin diffusion experiments on the fluorinated TMD, we have determined that the TMD forms a trimeric helical bundle. For the HIV gp4l MPER-TMD, we found the presence of a turn between the MPER helix and the TMD helix by measuring intramolecular distances and probing the lipid-peptide and water-peptide interactions. Intermolecular 19F- 19F distances of the fluorinated peptides indicate that the MPER-TMD is a trimeric. In addition to membrane fusion proteins, we have studied the oligomeric structure and the zinc-bound coordination geometry of a de novo designed amyloid fibril that catalyzes ester hydrolysis. By measuring the intermolecular contacts, we determined that peptides form parallel-in- register P-sheets and further assemble into stacked bilayers in an antiparallel orientation. The zinc binding sites were confirmed by the chemical shifts perturbation of histidines with zinc and the specific zinc-bound geometry was identified by measuring intra-residue distances of histidines. We also investigated the effects of cryoprotectants on the spectral resolution of lipid membranes and membrane peptides at low temperature. 13C and 1H MAS spectra of various cryoprotected membranes showed that DMSO provides the best resolution enhancement with the best ice formation retardation at low temperature and DLPE lipid exhibits the excellent resolution.
Download or read book Characterization of Structure and Dynamics of Membrane Proteins from Solid state NMR written by Byungsu Kwon and published by . This book was released on 2018 with total page 144 pages. Available in PDF, EPUB and Kindle. Book excerpt: Solid-state nuclear magnetic resonance (ssNMR) spectroscopy is an essential tool for elucidating the structure, dynamics, and function of biomolecules. ssNMR is capable of studying membrane proteins in near-native lipid bilayers and is thus preferred over other biophysical techniques for characterizing the structure and dynamics of membrane proteins. This thesis primarily focuses on the study of the following membrane proteins: 1) the N-terminal ectodomain and C-terminal cytoplasmic domain of influenza A virus M2 and 2) HIV-1 glycoprotein gp4l membrane-proximal external region and transmembrane domain (MPER-TMD) in a near native membrane environment. The cytoplasmic domain of M2 is necessary for membrane scission and virus shedding. The M2(22-71) construct shows random-coil chemical shifts, large motional amplitudes, and a membrane surface-bound location with close proximity to water, indicating the post-amphipathic helix (AH) cytoplasmic domain is a dynamic random coil near the membrane surface. The influenza M2 ectodomain contains highly conserved epitopes but its structure is largely unknown. The M2(1-49) construct containing both the ectodomain and transmembrane domain exhibits an entirely unstructured ectodomain with a motional gradient in which the motion is slower for residues near the TM domain, which attributed to the formation of a tighter helical bundle in the presence of drug that should cause the more tightened C-terminal ectodomain, thereby slowing its local motions. HIV-1 virus gp4l is directly involved in virus-cell membrane fusion. However, the structural topologies of the gp4l MPER-TMD are still controversial and the biologically-relevant intrinsic conformational state of MPER has not yet been determined. In order to obtain near native structural information of gp4l, we have studied gp41 (665-704) and found a primarily a-helical conformation, membrane-anchored trimeric TMD and water-exposed membrane surface-bound MPER. Intra- and intermolecular distances measured using 19C-19F REDOR and 19F-19F CODEX revealed that MPER-TMD has a significant kink between MPER and TMD, which has aided a deeper understanding of the HIV virus entry mechanism and the design of vaccines.
Download or read book Membrane Proteins Production for Structural Analysis written by Isabelle Mus-Veteau and published by Springer. This book was released on 2014-06-20 with total page 441 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book updates the latest development in production, stabilization and structural analysis techniques of membrane proteins. This field has made significant advances since the elucidation of the first 3-D structure of a recombinant G Protein Coupled Receptor (GPCR), rhodopsin, with the structure of several more GPCRs having been solved in the past five years. In fact, the 2012 Nobel Prize in Chemistry was awarded for groundbreaking discoveries on the inner workings of GPCRs. This book is essential reading for all researchers, biochemists and crystallographers working with membrane proteins, who are interested by the structural characterization of their favorite protein and who wish to follow the expression, migration, modifications and recycling of a membrane protein.
Download or read book Study of Bacteriorhodopsin in a Controlled Lipid Environment written by Vivien Yeh and published by Springer. This book was released on 2018-10-26 with total page 139 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book focuses on the study of how the properties of nanodiscs, such as lipid composition and size, influence the function of the embedding integral membrane protein, bacteriorhodopsin. The author performed systematic studies to show that the lipid composition and the charge of the hydrophobic head and the structure of hydrophilic tails affect the photocycle pathway of bacteriorhodopsin, which is closely associated with its proton-pumping activity. Furthermore, the author demonstrated a highly efficient method for extracting membrane proteins directly from the biological membrane, preserving protein conformation, function and essential native lipids. This book demonstrates optimization and sample preparation, and presents practical methods of preparing membrane protein-embedded nanodisc samples for biophysical studies, which benefit structural and functional studies in the field of membrane protein characterization, both.
