Information about Fiber Diffraction
Fiber diffraction is a scattering technique in which molecular structure is determined from scattering data (usually of X-rays or electrons) from filaments composed of a regular array of molecules distinguished by a single direction (the fiber axis).
The resulting diffraction patterns show layer lines, each with Bessel function intensities.
Historical role
Fiber diffraction data led to several important advances in the development of structural biology, e.g., the original models of the α-helix and the Watson-Crick model of double-stranded DNA.References
- Cochran W, Crick FHC, and Vand V (1952). "The Structure of Synthetic Polypeptides. I. The Transform of Atoms on a Helix". Acta Cryst., 5, 581-586.
External links
- Fiber Diffraction — an introduction provided by Prof. K.C. Holmes, Max Planck Institute for Medical Research, Heidelberg.
Protein structure determination methods | |
|---|---|
| High resolution | X-ray crystallography |
| Medium resolution | Cryo-electron microscopy |
| Spectroscopic | NMR |
| Translational Diffusion | Analytical ultracentrifugation |
| Rotational Diffusion | Fluorescence anisotropy |
| Chemical | Hydrogen-deuterium exchange |
| Thermodynamic | Equilibrium unfolding |
| Computational | Protein structure prediction |
Scattering is a general physical process whereby some forms of radiation, such as light, sound or moving particles, for example, are forced to deviate from a straight trajectory by one or more localized non-uniformities in the medium through which it passes.
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In mathematics, Bessel functions, first defined by the mathematician Daniel Bernoulli and generalized by Friedrich Bessel, are canonical solutions y(x) of Bessel's differential equation:
for an arbitrary real or complex number α.
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for an arbitrary real or complex number α.
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Structural biology is a branch of molecular biology concerned with the study of the architecture and shape of biological macromolecules—proteins and nucleic acids in particular—and what causes them to have the structures they have.
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alpha helix (α-helix) is a right-handed coiled conformation, resembling a spring, in which every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier ( hydrogen bonding). (See also helix.
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Protein structure, from primary to quaternary structure.]] Biochemistry refers to four distinct aspects of a protein's structure:
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- Primary structure - the amino acid sequence of the peptide chains.
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X-ray crystallography is the science of determining the arrangement of atoms within a crystal from the manner in which a beam of X-rays is scattered from the electrons within the crystal.
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Electron cryomicroscopy (sometimes called cryo-EM or often cryo-electron microscopy, although it is the microscope and specimen stage and not the electrons that are cold) is a form of electron microscopy (EM) where the sample is studied at cryogenic temperatures
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Protein nuclear magnetic resonance spectroscopy (usually abbreviated protein NMR) is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins.
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The ultracentrifuge is a centrifuge optimized for spinning a rotor at very high speeds, capable of generating acceleration as high as 1,000,000 g (9,800 km/s²). There are two kinds of ultracentrifuges, the preparative and the analytical ultracentrifuge.
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In chemistry, fluorescence anisotropy assays the rotational diffusion of a molecule from the decorrelation of polarization in fluorescence, i.e., between the exciting and emitted (fluorescent) photons.
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Hydrogen-deuterium exchange (also called H-D or H/D exchange) is a chemical reaction in which a covalently bonded hydrogen atom is replaced by a deuterium atom, or vice versa. Usually the examined protons are the amides in the backbone of a protein.
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In biochemistry, equilibrium unfolding is the process of unfolding a protein or RNA molecule by gradually changing its solution conditions, i.e., its environment. Since equilibrium is maintained at all steps, the process is reversible (equilibrium folding).
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Protein structure prediction is one of the most important goals pursued by bioinformatics and theoretical chemistry. Its aim is the prediction of the three-dimensional structure of proteins from their amino acid sequences, sometimes including additional relevant information such as
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