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The word revolution has a number of definitions (The American Heritage Dictionary, 2006). The one most pertinent to this series and volume is 'a sudden or momentous change in a situation'. Recent years have seen an unprecedented explosion of interest in unfolded proteins in all of their various forms. Coupled with this increase in interest we have seen momentous changes in the way unfolded proteins are viewed. Two particular paradigms have come under close scrutiny: unfolded proteins are disordered random coils devoid of persistent structure, and protein function first requires protein structure. The first of these is currently a hotly debated subject. The second paradigm we can safely claim...
Conventional CD8+ and CD4+ T cells recognize antigens, presented by antigen-presenting cells in the form of short peptides loaded onto major histocompatibility complex (MHC) class I and class II molecules, through their T cell receptor (TCR). Somatic gene rearrangement of the TCR locus and randomization of TCR hyper-variable regions generate the marked diversity of TCRs. Once assembled, the heterodimeric TCR confers specificity to naïve T cells. The naïve T cell repertoire of an individual is established by selection processes in the thymus and cannot be broadened upon antigen recognition by additional somatic mutations. In humans, the estimated number of distinct TCRs in the naïve T cell...
"This book highlights the use of systems approaches including genomic, cellular, proteomic, metabolomic, bioinformatics, molecular, and biochemical, to address fundamental questions in complex diseases like cancer diabetes but also in ageing"--Provided by publisher.
Dr. William E. Paul (1936–2015) was the leader of the National Institutes of Health (NIH) immunology community and his career is without parallel in the field of immunology. He was the Chief of the Laboratory of Immunology, National Institute of Allergy and Infectious Diseases (NIAID), from 1970 at the age of 34 until his death. His groundbreaking contributions to the field of immunology, including the discovery of interleukin (IL)-4, led to more than 600 publications over half a century. He also played an important role in the establishment of the NIH Vaccine Research Center while he was the Director of the NIH Office of AIDS Research. Furthermore, Dr. Paul was a shining icon and an inter...
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. - 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
This volume covers state-of-the-art applications of solid-state and solution nuclear magnetic resonance( NMR) spectroscopy to study protein structure, dynamics and interactions. Chapters detail various aspects of data acquisition and processing, determination of the structure, multi-timescale dynamics of entities ranging from individual proteins to large macromolecular complexes to intact viral assemblies. The final two chapters will highlight the promise of NMR beyond field strengths of 1 GHz to study the structure, dynamics and interactions of a larger class of proteins and protein complexes of extraordinary biological interest. Written in the highly successful Methods in Molecular Biology series format, chapters provide detailed laboratory protocols and troubleshooting tips that would be of great practical help to NMR spectroscopists with different levels of expertise.
This book provides an in-depth coverage not only of liver pathology but also of diagnosis of the numerous types of liver disease, placing specific emphasis on current treatments of liver pathology including the most up-to-date information on liver transplantation. The first part of provides an in-depth account of the liver pathology in different conditions such as Hepatits, liver ischaemia reperfusion injury, Lyme disease, cirrhotic cardiomyopathy and hepatocellular carcinoma. The second part provides a comprehensive overview of diagnostic methods. Of particular interest are chapters on the latest techniques in Patient-specific 3D printing and transient elastography (FibroScan). The final pa...
Janne Marie Soetbeer determines the optimal dynamical decoupling (DD) scheme for efficient reduction of electron spin coherence loss in model systems for spin labelled biomolecules depending on their particular relaxation behavior. Extending the nth order DD scheme to double electron-electron resonance (DEER) experiments require the addition of multiple pump pulses for ≠ 1. Incomplete excitation of pump spin packets introduce signal artefacts which are minimized by pump pulse optimization including linear-chirp and asymmetric hyperbolic secant pulses. Prolonging the dipolar evolution time with decreased signal artefact allows to extent the measurable interspin distances in biomolecules which were otherwise not accessible due to spin echo relaxation.