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Book Solid State Nuclear Magnetic Resonance Studies of the Structures Membrane Locations Cholesterol Contact and Membrane Motions of Membrane Associated HIV Fusion Peptide HFP

Download or read book Solid State Nuclear Magnetic Resonance Studies of the Structures Membrane Locations Cholesterol Contact and Membrane Motions of Membrane Associated HIV Fusion Peptide HFP written by Lihui Jia and published by . This book was released on 2017 with total page 295 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Solid State Nuclear Magnetic Resonance of the HIV 1 and Influenza Fusion Peptides Associated with Membranes

Download or read book Solid State Nuclear Magnetic Resonance of the HIV 1 and Influenza Fusion Peptides Associated with Membranes written by Michele L. Bodner and published by . This book was released on 2006 with total page 288 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Local Secondary Structure and Strand Arrangements of the Membrane associated HIV 1 Fusion Peptide Oligomers Probed by Solid state Nuclear Magnetic Resonance

Download or read book Local Secondary Structure and Strand Arrangements of the Membrane associated HIV 1 Fusion Peptide Oligomers Probed by Solid state Nuclear Magnetic Resonance written by Zhaoxiong Zheng and published by . This book was released on 2007 with total page 410 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book High Resolution Tertiary Structure of the Membrane associated HIV Fusion Peptides by Solid State Nuclear Magnetic Resonance

Download or read book High Resolution Tertiary Structure of the Membrane associated HIV Fusion Peptides by Solid State Nuclear Magnetic Resonance written by Scott Schmick and published by . This book was released on 2012 with total page 311 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book NMR Structural Studies of the Integral Membrane Protein Vpu from Hiv 1

Download or read book NMR Structural Studies of the Integral Membrane Protein Vpu from Hiv 1 written by Che Ma and published by . This book was released on 2000 with total page 88 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Temperature Dependence Structural Plasticity and Resonance Assignment of Uniformly Labeled HIV 1 Fusion Peptides Associated with Membranes

Download or read book Temperature Dependence Structural Plasticity and Resonance Assignment of Uniformly Labeled HIV 1 Fusion Peptides Associated with Membranes written by Michele L. Bodner and published by . This book was released on 2003 with total page 140 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Development of Solid state NMR Spectroscopy for Membrane Proteins and the Application to Vpu from HIV 1

Download or read book Development of Solid state NMR Spectroscopy for Membrane Proteins and the Application to Vpu from HIV 1 written by Eugene Chun-Chin Lin and published by . This book was released on 2015 with total page 148 pages. Available in PDF, EPUB and Kindle. Book excerpt: Solid-state nuclear magnetic resonance (NMR) spectroscopy is a robust method to solve the structures of membrane proteins in their native bilayer environments. Two systems have been well established: oriented samples (OS) are referred to proteins incorporated in the magnetic aligned bicelles, and rotationally aligned (RA) samples are referred to proteins undergoing fast rotational diffusion in proteoliposomes. 1H-15N and 1H-13C dipolar couplings are measured as the angular restraints for the structure calculations. New separated-local-field experiment, Dual-PISEMO, is developed for OS solid-state NMR to measure 1H-13C dipolar couplings of the uniformly 13C labeled proteins, which provide both backbone and side-chain conformations. In order to obtain the full assignments and restraints in OS solid-state NMR, 1H-irradiations with mismatched conditions are implemented to improve the crucial step: the magnetization transfer between 15N and 13C. Non-uniform sampling (NUS) is an alternative approach to further the experimental time of high-dimensional solid-state NMR experiments. Compressed sensing (CS) is able to reconstruct the spectra with 25 ~ 33% of data with the optimized sampling scheme, and covariance spectroscopy provides promising results with alternative States sampling scheme, which requires 50% of data or less. Viral protein "u" (Vpu) from HIV-1 is a type I membrane protein consisting of a transmembrane domain and a cytoplasmic domain, which are associated with different biological activities to enhance viral infectivity. It is essential to determine the three-dimensional structure of Vpu in order to understand its mechanisms in the molecular level and to develop new classes of anti-viral drugs. Magic-angle spinning (MAS) experiments providing high-sensitivity and high- resolution spectra, are implemented to study Vpu incorporated into proteoliposomes. 15N, 13C chemical shift and 1H-15N, 1H-13C dipolar couplings are measured and converted to equivalent structural restraints.

Book Solid state NMR Studies of Structure and Dynamics of HIV 1 Capsid CA Protein Assemblies

Download or read book Solid state NMR Studies of Structure and Dynamics of HIV 1 Capsid CA Protein Assemblies written by Yun Han and published by . This book was released on 2014 with total page 211 pages. Available in PDF, EPUB and Kindle. Book excerpt: There are around 34 million people in the world living with HIV-1, which is a causative agent of acquired immunodeficiency syndrome (AIDS). AIDS has become the ninth leading cause for death of people ages 25-34 in the US. Even though highly active antiretroviral therapy (HAART) showed effectiveness in suppressing the virus replication and significantly prolonged the patients lives, AIDS still remains an uncured disease. To develop new therapies, atomic-level understanding of the mechanism of HIV-1 lifecycle, including the structures of the various protein assemblies, is needed. The Gag polyprotein and its component capsid (CA) protein are essential constituents of the HIV-1 life cycle, and have recently attracted attention as targets for drug development. However, the atomic resolution structure and the dynamics of Gag and CA protein assemblies and their complexes with small-molecule inhibitors are not available because these assemblies are not amenable for characterization by traditional structural biology methods, X-ray diffraction and solution NMR spectroscopy. Solid-state NMR spectroscopy has the unique capability of providing atomic-level structural and dynamics information in large protein assemblies. The focus of this dissertation is establishing solid-state NMR spectroscopy as an atomic-level probe of structure and dynamics in HIV-1 protein assemblies. This effort required first establishing sample conditions for formation of HIV-1 protein assemblies that give rise to high-resolution solid-state NMR spectra for subsequent structural studies. In my Ph. D. work, I have optimized protocols to prepare homogeneous HIV-1 CA protein assemblies in vitro, developed confocal imaging method to characterize the morphologies of the resulting assemblies. With the suitable samples in hand, I have acquired solid-state NMR spectra on assemblies of CA protein and the maturation intermediate, CA-SP1, for structural analysis. Using these solid-state NMR data, I and my colleagues have obtained novel insights into the following aspects of HIV-1 structural biology: i) conformation of CA protein in conical assemblies; ii) the role of conformational dynamics of the hinge region in the structural polymorphism of CA in conical assemblies; iii) conformation of spacer peptide SP1 in tubular CA-SP1 assemblies; iv) conformation and dynamics of CA in tubular assemblies. In this thesis, I will first discuss the preparation and characterization of HIV-1 CA and CA-SP1 protein assemblies (Chapter 2 and 3). I will then describe the resonance assignments and secondary structure analysis of conical assemblies of HIV-1 CA protein (Chapter 4). Next, in Chapter 5, I will present the dynamics studies of conical assemblies of HIV-1 CA protein assemblies. In Chapter 6, I will discuss the resonance assignments and conformational analysis of tubular assemblies of HIV-1 CA and CA-SP1 proteins. The long-term goal of this research is developing comprehensive understanding of the mechanism of capsid assembly and disassembly, HIV-1 maturation, through the structural and dynamics analysis of the CA and Gag assemblies. The work discussed here represents the first step toward this goal and lays out the methodological and intellectual foundations enabling the solid-state NMR analysis of HIV-1 protein assemblies.

Book Functional and Structural Study of Vpu from HIV 1 by Nuclear Magnetic Resonance Spectroscopy

Download or read book Functional and Structural Study of Vpu from HIV 1 by Nuclear Magnetic Resonance Spectroscopy written by Hua Zhang and published by . This book was released on 2015 with total page 138 pages. Available in PDF, EPUB and Kindle. Book excerpt: Viral protein U (Vpu) is an 81-residue membrane protein encoded by HIV-1. It has two distinct domains, a hydrophobic transmembrane domain, which has been well studied, and a cytoplasmic helical domain with two conserved phosphorylation sites, which has proven to be more difficult to study in large part because of its dynamics. The two domains are associated with different biological activities that contribute to the pathogenicity of HIV-1 infections in humans. Vpu removes CD4 receptor from ER and causes its subsequent degradation to enhance viral infectivity. Vpu enhances release of newly formed virus particles from infected cells by antagonize human immune restriction factor BST-2. Recently, Vpu has also been discovered to interact with NK cell receptor NK-cell, T-cell and B-cell antigen (NTB-A) to induce down-modulation of NTB-A, and prevent HIV-Infected cells from degranulation and lysis by NK cells. A combination of solution and solid-state NMR experiments are used to determine the structure of cytoplasmic domain (VpuCyto) and full-length of Vpu in micelles and liposomes environment. Both constructs have a U-shape cytoplasmic domain that associated with the lipid environment. The second section describes the membrane anchoring property of W76 in the C-terminus of Vpu. Biological study found that W76 is specifically important for the enhancement of virion release, and NMR data suggests that W76 might function by interacting directly with the lipid bilayer. Significant intensity change and chemical shift perturbation were observed for W76 upon addition of liposomes to VpuCyto; in addition, paramagnetic relaxation enhancement (PRE) indicates that the residue is embedded in the interior of micelles. The last section describes the interaction between transmembrane domains of Vpu and NTB-A base on a combination of biological, NMR spectroscopic and computational methods. The knowledge about the transmembrane domain of Vpu (VpuTM) enables detailed studies of its interactions with NTB-A. NMR spectral changes demonstrate that specific residues in VpuTM interact with specific residues in the transmembrane domains of NTB-A. A model of the complex is generated by docking, with the input of interaction faces base on NMR and biological results.

Book Structural and Functional Study of Virus Protein u from HIV 1 by Nuclear Magnetic Resonance Spectroscopy

Download or read book Structural and Functional Study of Virus Protein u from HIV 1 by Nuclear Magnetic Resonance Spectroscopy written by Yan Wang and published by . This book was released on 2012 with total page 92 pages. Available in PDF, EPUB and Kindle. Book excerpt: Virus protein 'u' (Vpu) is one of the accessory proteins expressed by the HIV-1 genome. It is a type I integral phosphoprotein which contains a single-helical transmembrane (TM) domain and an amphipathic cytoplasmic domain. In its oligomeric form, the transmembrane domain is responsible for the ion channel activity of Vpu, and the domain itself is the main contributor in the antagonistic function against BST-2, a host cell viral restriction factor. The cytoplasmic domain is responsible for the binding of CD4 receptors at the endoplasmic reticulum (ER) and recruiting other protein complexes that ultimately leads to the CD4 degradation through the ubiquitin-proteasome degradation pathway. In order to structurally characterize this protein by NMR, a lipid environment in the form of either micelle or bicelle was used for the proper solubilization and folding of the protein. Solution NMR was used as a method to quickly examine the stability of the protein within micelles and to identify the secondary structure regions, while solid-state NMR gave helical tilt and rotation information as well as the orientation restraints of individual amide bonds for a protein embedded in a bilayer environment. In this thesis, structural features of Vpu based on NMR results of wildtype and various truncated/mutant forms of the protein are presented. A single site mutation on the TM that enables the inter-conversion of structure and functionality between Vpu and M2, a structural analogue from Influenza A virus, will be discussed. The last section will describe the collaborative effort of examining the protein-protein interaction between Vpu and BST-2 using a combination of spectroscopic, biological, and computational approaches. Residues involved in the interaction between the two proteins' TM domains were identified in solution NMR experiments while the helical tilt angles and interaction faces were determined by solid-state NMR. A model of the complex is presented and shows remarkable agreement with the combination of NMR data, biological results, and computational simulation.

Book Nmr In Structural Biology A Collection Of Papers By Kurt Wuthrich

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.

Book Membrane Fusion Studies with Solid State NMR

Download or read book Membrane Fusion Studies with Solid State NMR written by Prashant Radheshyam Agrawal and published by . This book was released on 2007 with total page 128 pages. Available in PDF, EPUB and Kindle. Book excerpt: