Information about Flow Birefringence
In biochemistry, flow birefringence is a hydrodynamic technique for measuring the rotational diffusion constants (or, equivalently, the rotational drag coefficients. The birefringence of a solution sandwiched between two concentric cylinders is measured as a function of the difference in rotational speed between the inner and outer cylinders. The flow tends to orient an ellipsoidal particle (typically, a protein, virus, etc.) in one direction, whereas rotational diffusion (tumbling) causes the molecule to become disoriented. The equilibrium between these two processes as a function of the flow provides a measure of the axial ratio of the ellipsoidal particle.
See also
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 |
Biochemistry is the study of the chemical processes in living organisms.[1] The word "biochemistry" comes from the Greek word βιοχημεία biochēmeia, which means "the chemistry of life.
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Hydrodynamics, also known as liquid-dynamics in limited academic circles, (literally, "water motion") is fluid dynamics applied to liquids, such as water, alcohol, oil, and blood. However, this distinction from fluid dynamics as a whole is not always fully observed.
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Birefringence, or double refraction, is the decomposition of a ray of light into two rays (the ordinary ray and the extraordinary ray) when it passes through certain types of material, such as calcite crystals or boron nitride, depending on the polarization of
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In hydrodynamics, the Perrin friction factors are multiplicative adjustments to the translational and rotational friction of a rigid spheroid, relative to the corresponding frictions in spheres of the same volume. These friction factors were first calculated by Jean-Baptiste Perrin.
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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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