Several infectious diseases, such as polio, measles, diphtheria, rubella, mumps and tetanus can b... more Several infectious diseases, such as polio, measles, diphtheria, rubella, mumps and tetanus can be controlled and, in many cases, be eradicated with current vaccines.
Lower respiratory tract infections due to human respiratory syncytial viruses (HRSV) continue to ... more Lower respiratory tract infections due to human respiratory syncytial viruses (HRSV) continue to threat human beings. The virus causes seasonal epidemics and infects humans of different age groups. Neonates and immunocompromised individuals are more prone to severe HRSV infection that may require hospitalization and in many cases lead to death. According to worldwide estimations, millions of HRSV infection were reported in both developed and developing countries.
For further information see our web site at www.rsc.org vi Preface backbone and side-chain placem... more For further information see our web site at www.rsc.org vi Preface backbone and side-chain placement, NMR also provides dynamic (ensemble) information and crystallography provides a 'snapshot' and is often considered static. Solution approaches, such as limited proteolysis combined with mass spectrometry and small-angle scattering approaches (Chapter 3), also provide dynamic information. In cryo-ET and cryo-electron microscopy (cryo-EM) (Chapter 5), macromolecules are frozen in their native state, allowing for discrete selection of dynamic states to be visualized, albeit at lower resolution. Generally, NMR spectroscopy is utilized for small protein molecules that are flexible, X-ray crystallography for medium-sized proteins and complexes that are compact, whereas very large macromolecular assemblages or membranous protein structures are determined by cryo-EM. The largest issue separating cryo-EM and cryo-ET from crystallography, in addition to size and the limitations of crystal formation, is resolution. Cryo-EM has generally been considered a low-resolution technique, giving reconstructions around 15-30 Å , but with advances in sample handling, instrumentation, image processing and model building, near-atomic resolution structures are now being achieved. For cryo-ET the resolution achieveable is still low. In reality, hybrid approaches, combining NMR, X-ray crystallography and cryo-EM, cryo-ET and solution data, are often adopted, which provides a powerful means of filling gaps which can arise in the structural characterization of large macromolecules. For example, in studies where large viruses cannot be crystallized, subcomponents can be crystallized to obtain high-resolution information, which can then be used to interpret the structure at lower resolution obtained by cryo-EM or cryo-ET. Or atomic structures obtained from homologous viral proteins/virus capsids can be used for 3D homology model building. These approaches permit the pseudo-atomic visualization of interaction interfaces between protein-protein subunits, protein-nucleic acids and protein-lipid in virus capsids and also the visualization of virus capsid-host interactions.
How Pathogenic Viruses Think: Making Sense of Virology, Second Edition, is an independent publica... more How Pathogenic Viruses Think: Making Sense of Virology, Second Edition, is an independent publication and has not been authorized, sponsored, or otherwise approved by the owners of the trademarks or service marks referenced in this product.
For further information see our web site at www.rsc.org vi Preface backbone and side-chain placem... more For further information see our web site at www.rsc.org vi Preface backbone and side-chain placement, NMR also provides dynamic (ensemble) information and crystallography provides a 'snapshot' and is often considered static. Solution approaches, such as limited proteolysis combined with mass spectrometry and small-angle scattering approaches (Chapter 3), also provide dynamic information. In cryo-ET and cryo-electron microscopy (cryo-EM) (Chapter 5), macromolecules are frozen in their native state, allowing for discrete selection of dynamic states to be visualized, albeit at lower resolution. Generally, NMR spectroscopy is utilized for small protein molecules that are flexible, X-ray crystallography for medium-sized proteins and complexes that are compact, whereas very large macromolecular assemblages or membranous protein structures are determined by cryo-EM. The largest issue separating cryo-EM and cryo-ET from crystallography, in addition to size and the limitations of crystal formation, is resolution. Cryo-EM has generally been considered a low-resolution technique, giving reconstructions around 15-30 Å , but with advances in sample handling, instrumentation, image processing and model building, near-atomic resolution structures are now being achieved. For cryo-ET the resolution achieveable is still low. In reality, hybrid approaches, combining NMR, X-ray crystallography and cryo-EM, cryo-ET and solution data, are often adopted, which provides a powerful means of filling gaps which can arise in the structural characterization of large macromolecules. For example, in studies where large viruses cannot be crystallized, subcomponents can be crystallized to obtain high-resolution information, which can then be used to interpret the structure at lower resolution obtained by cryo-EM or cryo-ET. Or atomic structures obtained from homologous viral proteins/virus capsids can be used for 3D homology model building. These approaches permit the pseudo-atomic visualization of interaction interfaces between protein-protein subunits, protein-nucleic acids and protein-lipid in virus capsids and also the visualization of virus capsid-host interactions.
How Pathogenic Viruses Think: Making Sense of Virology, Second Edition, is an independent publica... more How Pathogenic Viruses Think: Making Sense of Virology, Second Edition, is an independent publication and has not been authorized, sponsored, or otherwise approved by the owners of the trademarks or service marks referenced in this product.
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