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Helical Wheel
A helical wheel is a type of Plot (graphics), plot or visual representation used to illustrate the properties of alpha helix, alpha helices in proteins. The primary sequence, sequence of amino acids that make up a helical region of the protein's secondary structure are plotted in a rotating manner where the angle of rotation between consecutive amino acids is 100°, so that the final representation looks down the helical axis. Polarity and Characteristics The plot reveals whether hydrophobic amino acids are concentrated on one side of the helix, usually with polarity (chemistry), polar or hydrophilic amino acids on the other. This arrangement is common in Alpha helix, alpha helices within globular proteins, where one face of the helix is oriented toward the hydrophobic core and one face is oriented toward the solvent-exposed surface. Specific patterns characteristic of tertiary structure, protein folds and protein-protein interaction, protein docking motifs are also revealed, a ...
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Helical Wheel
A helical wheel is a type of Plot (graphics), plot or visual representation used to illustrate the properties of alpha helix, alpha helices in proteins. The primary sequence, sequence of amino acids that make up a helical region of the protein's secondary structure are plotted in a rotating manner where the angle of rotation between consecutive amino acids is 100°, so that the final representation looks down the helical axis. Polarity and Characteristics The plot reveals whether hydrophobic amino acids are concentrated on one side of the helix, usually with polarity (chemistry), polar or hydrophilic amino acids on the other. This arrangement is common in Alpha helix, alpha helices within globular proteins, where one face of the helix is oriented toward the hydrophobic core and one face is oriented toward the solvent-exposed surface. Specific patterns characteristic of tertiary structure, protein folds and protein-protein interaction, protein docking motifs are also revealed, a ...
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Hydrophobic Core
The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and exclude water molecules. The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes hydrogen bonding between molecules of water and minimizes the area of contact between water and nonpolar molecules. In terms of thermodynamics, the hydrophobic effect is the free energy change of water surrounding a solute. A positive free energy change of the surrounding solvent indicates hydrophobicity, whereas a negative free energy change implies hydrophilicity. The hydrophobic effect is responsible for the separation of a mixture of oil and water into its two components. It is also responsible for effects related to biology, including: cell membrane and vesicle formation, protein folding, insertion of membrane proteins into the nonpolar lipid environment and protein-small molecule associations. Hence the ...
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Protein Structure
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers specifically polypeptides formed from sequences of amino acids, the monomers of the polymer. A single amino acid monomer may also be called a ''residue'' indicating a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is t ...
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Adobe Flash
Adobe Flash (formerly Macromedia Flash and FutureSplash) is a multimedia Computing platform, software platform used for production of Flash animation, animations, rich web applications, application software, desktop applications, mobile apps, mobile games, and embedded web browser video players. Flash displays text, vector graphics, and raster graphics to provide animations, video games, and applications. It allows streaming of Flash Video, audio and video, and can capture mouse, keyboard, microphone, and camera input. Digital art, Artists may produce Flash graphics and animations using Adobe Animate (formerly known as Adobe Flash Professional). Programmer, Software developers may produce applications and video games using Adobe Flash Builder, FlashDevelop, Flash Catalyst, or any text editor combined with the Apache Flex SDK. End users view Flash content via Adobe Flash Player, Flash Player (for web browsers), Adobe AIR (for desktop or mobile apps), or third-party players such as ...
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R (programming Language)
R is a programming language for statistical computing and graphics supported by the R Core Team and the R Foundation for Statistical Computing. Created by statisticians Ross Ihaka and Robert Gentleman, R is used among data miners, bioinformaticians and statisticians for data analysis and developing statistical software. Users have created packages to augment the functions of the R language. According to user surveys and studies of scholarly literature databases, R is one of the most commonly used programming languages used in data mining. R ranks 12th in the TIOBE index, a measure of programming language popularity, in which the language peaked in 8th place in August 2020. The official R software environment is an open-source free software environment within the GNU package, available under the GNU General Public License. It is written primarily in C, Fortran, and R itself (partially self-hosting). Precompiled executables are provided for various operating systems. R ...
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Coiled Coil
A coiled coil is a structural motif in proteins in which 2–7 alpha-helices are coiled together like the strands of a rope. (Dimers and trimers are the most common types.) Many coiled coil-type proteins are involved in important biological functions, such as the regulation of gene expression — e.g., transcription factors. Notable examples are the oncoproteins c-Fos and c-Jun, as well as the muscle protein tropomyosin. Discovery The possibility of coiled coils for α-keratin was initially somewhat controversial. Linus Pauling and Francis Crick independently came to the conclusion that this was possible at about the same time. In the summer of 1952, Pauling visited the laboratory in England where Crick worked. Pauling and Crick met and spoke about various topics; at one point, Crick asked whether Pauling had considered "coiled coils" (Crick came up with the term), to which Pauling said he had. Upon returning to the United States, Pauling resumed research on the topic. He conc ...
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Leucine Zipper
A leucine zipper (or leucine scissors) is a common three-dimensional structural motif in proteins. They were first described by Landschulz and collaborators in 1988 when they found that an enhancer binding protein had a very characteristic 30-amino acid segment and the display of these amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. The polypeptide segments containing these periodic arrays of leucine residues were proposed to exist in an alpha-helical conformation and the leucine side chains from one alpha helix interdigitate with those from the alpha helix of a second polypeptide, facilitating dimerization. Leucine zippers are a dimerization motif of the bZIP (Basic-region leucine zipper) class of eukaryotic transcription factors. The bZIP domain is 60 to 80 amino acids in length with a highly conserved DNA binding basic region and a more diversified leucin ...
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Tertiary Structure
Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure.Branden C. and Tooze J. "Introduction to Protein Structure" Garland Publishing, New York. 1990 and 1991. A number of tertiary structures may fold into a quaternary structure.Kyte, J. "Structure in Protein Chemistry." Garland Publishing, New York. 1995. History The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of polypept ...
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Solvent
A solvent (s) (from the Latin '' solvō'', "loosen, untie, solve") is a substance that dissolves a solute, resulting in a solution. A solvent is usually a liquid but can also be a solid, a gas, or a supercritical fluid. Water is a solvent for polar molecules and the most common solvent used by living things; all the ions and proteins in a cell are dissolved in water within the cell. The quantity of solute that can dissolve in a specific volume of solvent varies with temperature. Major uses of solvents are in paints, paint removers, inks, and dry cleaning. Specific uses for organic solvents are in dry cleaning (e.g. tetrachloroethylene); as paint thinners (toluene, turpentine); as nail polish removers and solvents of glue (acetone, methyl acetate, ethyl acetate); in spot removers (hexane, petrol ether); in detergents ( citrus terpenes); and in perfumes (ethanol). Solvents find various applications in chemical, pharmaceutical, oil, and gas industries, including in chemical syn ...
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Globular Protein
In biochemistry, globular proteins or spheroproteins are spherical ("globe-like") proteins and are one of the common protein types (the others being fibrous, disordered and membrane proteins). Globular proteins are somewhat water-soluble (forming colloids in water), unlike the fibrous or membrane proteins. There are multiple fold classes of globular proteins, since there are many different architectures that can fold into a roughly spherical shape. The term globin can refer more specifically to proteins including the globin fold. Globular structure and solubility The term globular protein is quite old (dating probably from the 19th century) and is now somewhat archaic given the hundreds of thousands of proteins and more elegant and descriptive structural motif vocabulary. The globular nature of these proteins can be determined without the means of modern techniques, but only by using ultracentrifuges or dynamic light scattering techniques. The spherical structure is induc ...
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Plot (graphics)
A plot is a graphical technique for representing a data set, usually as a graph showing the relationship between two or more variables. The plot can be drawn by hand or by a computer. In the past, sometimes mechanical or electronic plotters were used. Graphs are a visual representation of the relationship between variables, which are very useful for humans who can then quickly derive an understanding which may not have come from lists of values. Given a scale or ruler, graphs can also be used to read off the value of an unknown variable plotted as a function of a known one, but this can also be done with data presented in tabular form. Graphs of functions are used in mathematics, sciences, engineering, technology, finance, and other areas. Overview Plots play an important role in statistics and data analysis. The procedures here can broadly be split into two parts: quantitative and graphical. Quantitative techniques are the set of statistical procedures that yield numeric or ...
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