By Carol L. Nilsson
Lectins: Analytical applied sciences covers either analytical and organic elements of lectins (functional carbohydrate (complex sugar) acceptance proteins) and gives researchers within the box with a source containing history details and 'look-up' tables detailing lectin specificity and buildings. additionally integrated are equipment and sensible suggestions for designing new lectins from current non-lectin proteins, automatic ways to lectin proteomics and excessive answer mass spectrometry techniques.This publication might be of curiosity to either amateur and complicated researchers in biomedical, analytical and pharmaceutical fields who're curious about the examine of lectin constructions or who make the most of lectins as analytical instruments. The examine of lectins and their employment in analytical settings spans more than a few fields including:* Crystallography and lectin constitution databases* Carbohydrate microarrays for lectin characterization and glycotope identity* Proteomic methods to the practical identity of bacterial adhesins* iteration of lectins from enzymes* Probing cell-surface lectins with neoglycoconjugates* studies up to date suggestions, together with sensible tricks for laboratory paintings* presents evaluate of lectin e-resources and a number of other colour illustrations* encompasses a 'look-up' desk detailing lectin specificity
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Additional resources for Lectins: Analytical Technologies
G. on the cell surface. Several methods exist that allow the detailed three-dimensional characterization of protein structures and their ligand complexes, such as NMR, X-ray crystallography, neutron diffraction, and electron microscopy. Each of these methods has their weaknesses and strengths and they all complement each other. Two of the methods stand out, as they are the most widely used. These are X-ray crystallography and NMR (the latter method is discussed in Chapter 3). These two methods are sensitive to totally different physical properties of the molecules: while NMR detects signals related to the magnetic spin of the nuclei, X-ray crystallography relies on the diffraction of X-rays by the electrons of the atoms.
This method, also requiring the introduction of heavy atoms, is similar to the traditional MIR method, but it makes use of the anomalous scattering of heavy atoms at the absorption edge. Instead of collecting several datasets of different isomorphous heavy-atom derivatives and comparing them with the X-ray data from the native, unmodified protein crystal, datasets are collected from, ideally, one (derivatized) crystal, at several different wavelengths. qxd 5/28/2007 18:17 Page 19 Crystallography and Lectin Structure Database 19 weaker heavy-atom scatterers and has become increasingly popular in recent years .
After pioneering work on tachylectin from horseshoe crab , the crystal structures of eel lectin (fucolectin) and then snail agglutinin (HPA) have been solved, revealing new folds and new binding modes towards carbohydrates [88, 89]. In both cases, a trimeric arrangement organizes the binding sites in an optimal fashion for binding to the surface of bacteria. 1. Fungal lectins To date, only few structures of fungal lectins have been solved (Fig. 5). So far, the focus has mainly been on lectins that can be extracted from the fruiting bodies or from the mycelium of mushrooms.
Lectins: Analytical Technologies by Carol L. Nilsson