Alpha helix in the context of "GABAA receptor"

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⭐ Core Definition: Alpha helix

An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix).

The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure, and it is the local structure that is most easily predicted from a sequence of amino acids.

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Alpha helix in the context of Biomolecule

A biomolecule or biological molecule is loosely defined as a molecule produced by a living organism and essential to one or more typically biological processes. Biomolecules include large macromolecules such as proteins, carbohydrates, lipids, and nucleic acids, as well as small molecules such as vitamins and hormones. A general name for this class of material is biological materials. Biomolecules are an important element of living organisms. They are often endogenous, i.e. produced within the organism, but organisms usually also need exogenous biomolecules, for example certain nutrients, to survive.

Biomolecules and their reactions are studied in biology and its subfields of biochemistry and molecular biology. Most biomolecules are organic compounds, and just four elementsoxygen, carbon, hydrogen, and nitrogen—make up 96% of the human body's mass. But many other elements, such as the various biometals, are also present in small amounts.

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Alpha helix in the context of William Astbury

William Thomas Astbury FRS (25 February 1898 – 4 June 1961) was an English physicist and molecular biologist who made pioneering X-ray diffraction studies of biological molecules. His work on keratin provided the foundation for Linus Pauling's discovery of the α-helix. He also studied the structure for DNA in 1937 and made the first step in the elucidation of its structure.

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Alpha helix in the context of Protein

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.

A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; but in certain organisms the genetic code can include selenocysteine and—in certain archaeapyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by post-translational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Some proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can work together to achieve a particular function, and they often associate to form stable protein complexes.

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Alpha helix in the context of Helix

A helix (/ˈhlɪks/; pl.helices) is a shape like a cylindrical coil spring or the thread of a machine screw. It is a type of smooth skew curve with tangent lines at a constant angle to a fixed axis. Helices are important in biology, as the DNA molecule is formed as two intertwined helices, and many proteins have helical substructures, known as alpha helices. The word helix comes from the Greek word ἕλιξ, "twisted, curved". A "filled-in" helix – for example, a "spiral" (helical) ramp – is a surface called a helicoid.

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Alpha helix in the context of Linus Pauling

Linus Carl Pauling FRS (/ˈpɔːlɪŋ/ PAW-ling; February 28, 1901 – August 19, 1994) was an American chemist and peace activist. He published more than 1,200 papers and books, of which about 850 dealt with scientific topics. New Scientist called him one of the 20 greatest scientists of all time. For his scientific work, Pauling was awarded the Nobel Prize in Chemistry in 1954. For his peace activism, he was awarded the Nobel Peace Prize in 1962. He is one of five people to have won more than one Nobel Prize. Of these, he is the only person to have been awarded two unshared Nobel Prizes, and one of two people to be awarded Nobel Prizes in different fields, the other being Marie Skłodowska-Curie.

Pauling was one of the founders of the fields of quantum chemistry and molecular biology. His contributions to the theory of the chemical bond include the concept of orbital hybridisation and the first accurate scale of electronegativities of the elements. Pauling also worked on the structures of biological molecules, and showed the importance of the alpha helix and beta sheet in protein secondary structure. Pauling's approach combined methods and results from X-ray crystallography, molecular model building, and quantum chemistry. His discoveries inspired the work of Rosalind Franklin, James Watson, Francis Crick, and Maurice Wilkins on the structure of DNA, which in turn made it possible for geneticists to crack the DNA code of all organisms.

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Alpha helix in the context of Alpha-keratin

Alpha-keratin, or α-keratin, is a type of keratin found in mammalian vertebrates. This protein is the primary component in hairs, horns, claws, nails and the epidermis layer of the skin. α-keratin is a fibrous structural protein, meaning it is made up of amino acids that form a repeating secondary structure. The secondary structure of α-keratin is very similar to that of a traditional protein α-helix and forms a coiled coil. Due to its tightly wound structure, it can function as one of the strongest biological materials and has various functions in mammals, from predatory claws to hair for warmth. α-keratin is synthesized through protein biosynthesis, utilizing transcription and translation, but as the cell matures and is full of α-keratin, it dies, creating a strong non-vascular unit of keratinized tissue.

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Alpha helix in the context of Biomolecular structure

Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function. The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits. This useful distinction among scales is often expressed as a decomposition of molecular structure into four levels: primary, secondary, tertiary, and quaternary. The scaffold for this multiscale organization of the molecule arises at the secondary level, where the fundamental structural elements are the molecule's various hydrogen bonds. This leads to several recognizable domains of protein structure and nucleic acid structure, including such secondary-structure features as alpha helixes and beta sheets for proteins, and hairpin loops, bulges, and internal loops for nucleic acids.The terms primary, secondary, tertiary, and quaternary structure were introduced by Kaj Ulrik Linderstrøm-Lang in his 1951 Lane Medical Lectures at Stanford University.

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