By Elizabeth Yuriev, Paul A. Ramsland
Structural Glycobiology covers the experimental, theoretical, and substitute applied sciences utilized in the research of the structural foundation for the various organic roles of carbohydrates. The booklet overviews the applying of specialised applied sciences to the examine of carbohydrates in biology, stories suitable and present examine within the box, and is illustrated all through by way of particular examples of the way examine investigations have yielded key structural and linked organic info on carbohydrates and glycolipids. specifically, the ebook focuses on:
- X-ray crystallography and small-angle scattering, NMR, and cryo-electron microscopy techniques
- Theoretical (modeling-based) ways, equivalent to molecular mechanics, molecular dynamics, loose strength calculations, and carbohydrate docking
- Alternative thoughts for yielding structural details on carbohydrates from advanced organic samples
- Carbohydrates in medication, particularly in parts which have been without delay impacted via our figuring out of the structural position of carbohydrates in immune attractiveness: melanoma, organ transplantation, and infection
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Extra resources for Structural glycobiology
2003). 80 Å resolution, PDB ID: 1BOS (Ling et al. 1998). 25 Å resolution, PDB ID: 3S6X (Reiter et al. 2011). Proteins are shown as ribbon-style representations and separate polypeptide chains in the oligomers are colored differently. Carbohydrate ligands are displayed as space-filling spheres in green. protein of reovirus, which binds to sialyated glycans on host cells. The crystal structure of σ1 in complex with 3′-sialyllactose (Reiter et al. 5d). 2011). Clearly, the diversity of oligomeric assemblies within host and pathogen carbohydrate-binding proteins (illustrated here by only a few examples) highlights the need to study the full-length proteins in their near physiological states.
Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique to study protein–glycan recognition. Different from the detailed atomic picture of molecules arranged in a crystalline array that is provided by x-ray crystallography (Chapter 1), NMR spectroscopy yields structural and dynamic information about molecules in solution. Both methods, naturally, have advantages and disadvantages. The first and most unpredictable requirement for any crystallographic study is the necessity to grow welldiffracting single crystals of the complexes.
The selective deuteration of one component of a complex is very powerful for probing the shape of protein–protein complexes in solution as the incorporation of nonexchangeable 2H into one protein enables a contrast difference to be set up between the 1H and deuterated components of a complex and subsequent separation of their match points in solution (Jeffries and Trewhella 2012). Aside from obtaining Rg, Dmax, and P(r) versus r, that in themselves can provide valuable insights into the solution states of macromolecules, what is of most interest to structural biologists is obtaining a sensible consensus model, or series of models, that best fit their scattering data.