About the Book
Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Pages: 145. Chapters: X-ray crystallography, Protein structure prediction, Structural alignment, Homology modeling, Bimolecular fluorescence complementation, Function-spacer-lipid construct, Green fluorescent protein, Nuclear magnetic resonance spectroscopy of proteins, Gel electrophoresis, Immunoprecipitation, Western blot, Surround Optical Fiber Immunoassay, Protein purification, Methylated DNA immunoprecipitation, Methods to investigate protein-protein interactions, Enzyme assay, Immunohistochemistry, Protein subcellular localization prediction, ChIP-on-chip, Kodecyte, Chromatin immunoprecipitation, Coomassie Brilliant Blue, Eastern blotting, Protein pKa calculations, Structure validation, Macromolecular crowding, Threading (protein sequence), Protein sequencing, List of protein structure prediction software, ChIP-exo, Phi value analysis, Peptide microarray, Gel electrophoresis of proteins, De novo protein structure prediction, Dead-end elimination, Immunostaining, Microscale thermophoresis, Kaede (protein), Peptide mass fingerprinting, ChIP-sequencing, Graphical models for protein structure, Electrophoretic mobility shift assay, Particle-induced X-ray emission, Chevron plot, Immunocytochemistry, Bradford protein assay, Strep-tag, Streptamer, Immunoelectrophoresis, Dual polarization interferometry, Chou-Fasman method, Aequorin, Capillary electrochromatography, Isoelectric focusing, GOR method, Loop modeling, Self-consistent mean field (biology), Site-directed spin labeling, CLIP-Seq, SDD-AGE, Columnmaster 4000, Biuret test, Activity-based proteomics, Magnet-assisted transfection, Photoactivatable fluorescent protein, Isobaric tag for relative and absolute quantitation, Lowry protein assay, Electroblotting, HNCOCA experiment, HNCA experiment, Expanded bed adsorption, PAR-CLIP, Far-western blotting, Isopeptag, TimeSTAMP protein labelling, Synapto-pHluorin, Helical wheel, Mammalian promoter database. Excerpt: X-ray crystallography is a method used for determining the atomic and molecular structure of a crystal, in which the crystalline atoms cause a beam of X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their disorder and various other information. Since many materials can form crystals-such as salts, metals, minerals, semiconductors, as well as various inorganic, organic and biological molecules-X-ray crystallography has been fundamental in the development of many scientific fields. In its first decades of use, this method determined the size of atoms, the lengths and types of chemical bonds, and the atomic-scale differences among various materials, especially minerals and alloys. The method also revealed the structure and function of many biological molecules, including vitamins, drugs, proteins and nucleic acids such as DNA. X-ray crystallography is still the chief method for characterizing the atomic structure of new materials and in discerning materials that appear similar by other experiments. X-ray crystal structures can also account for unusual electronic or elastic properties of a material, shed light on chemical interactions and processes, or serve as the basis for designing pharmaceuticals against diseases. In an X-ray diffraction measurement, a crystal is mounted on a goniometer and gradually rotated while being bombarded with X-rays, producing a diffraction pattern of regularly spaced spots known as reflections. The two-dimensional images taken at different rotations are converted into a three-dimensional model of the density of electrons within the crystal using the...
