Peptitergents
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Peptitergents
Peptitergents (a portmanteau of peptide and detergent) are synthetic peptides designed to be lipophilic on one side and hydrophilic on the other upon folding to an α-helical conformation and were designed to solubilize integral membrane protein An integral, or intrinsic, membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins can be classified as IMPs, but not all IMPs are transmembrane proteins. IMPs comp ...s in aqueous solution. They can be considered a sub-class of amphipols and are based on earlier fundamental explorations of amphiphilic secondary structures See also * Amphipols References Zwitterionic surfactants {{organic-compound-stub ...
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Amphipols
Amphipols (a portmanteau of amphiphilic polymers) are a class of amphiphilic polymers designed to keep membrane proteins soluble in water without the need for detergents, which are traditionally used to this end but tend to be denaturing. Amphipols adsorb onto the hydrophobic transmembrane surface of membrane proteins thanks to their hydrophobic moieties and keep the complexes thus formed water-soluble thanks to the hydrophilic ones. Amphipol-trapped membrane proteins are, as a rule, much more stable than detergent-solubilized ones, which facilitates their study by most biochemical and biophysical approaches. Amphipols can be used to fold denatured membrane proteins to their native form and have proven particularly precious in the field of single-particle electron cryo-microscopy (cryo-EM; see ''e.g.'' ).The properties and uses of amphipols and other non-conventional surfactants are the subject of a book by Jean-Luc Popot.Popot, J.-L. (2018) Membrane proteins in aqueous solutions. ...
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Portmanteau
In linguistics, a blend—also known as a blend word, lexical blend, or portmanteau—is a word formed by combining the meanings, and parts of the sounds, of two or more words together.Garner's Modern American Usage
p. 644.
English examples include '' smog'', coined by blending ''smoke'' and ''fog'', and '''', from ''motor'' ('' motorist'') and ''hotel''. A blend is similar to a
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Peptide
Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. Peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyclic peptides have an N-terminal (amine group) and C-terminal (carboxyl g ...
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Detergent
A detergent is a surfactant or a mixture of surfactants with Cleanliness, cleansing properties when in Concentration, dilute Solution (chemistry), solutions. There are a large variety of detergents. A common family is the alkylbenzene sulfonates, which are soap-like compounds that are more soluble than soap in hard water, because the polar sulfonate is less likely than the polar carboxylate of soap to bind to calcium and other ions found in hard water. Definitions The word ''detergent'' is derived from the Latin adjective , from the verb , meaning to wipe or polish off. Detergent can be defined as a surfactant or a mixture of surfactants with cleansing properties when in Concentration, dilute Solution (chemistry), solutions. However, conventionally, detergent is used to mean synthetic cleaning compounds as opposed to ''soap'' (a salt of the natural fatty acid), even though soap is also a detergent in the true sense. In domestic contexts, the term ''detergent'' refers to househ ...
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Lipophilic
Lipophilicity (from Greek language, Greek λίπος "fat" and :wikt:φίλος, φίλος "friendly") is the ability of a chemical compound to dissolve in fats, oils, lipids, and non-polar solvents such as hexane or toluene. Such compounds are called lipophilic (translated as "fat-loving" or "fat-liking"). Such non-polar solvents are themselves lipophilic, and the adage "like dissolves like" generally holds true. Thus lipophilic substances tend to dissolve in other lipophilic substances, whereas hydrophilic ("water-loving") substances tend to dissolve in water and other hydrophilic substances. Lipophilicity, hydrophobicity, and non-polarity may describe the same tendency towards participation in the London dispersion force, as the terms are often used interchangeably. However, the terms "lipophilic" and "hydrophobicity, hydrophobic" are not synonymous, as can be seen with silicones and fluorocarbons, which are hydrophobic but not lipophilic. __TOC__ Surfactants Hydrocarbon-based ...
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Hydrophilic
A hydrophile is a molecule or other molecular entity that is attracted to water molecules and tends to be dissolved by water.Liddell, H.G. & Scott, R. (1940). ''A Greek-English Lexicon'' Oxford: Clarendon Press. In contrast, hydrophobes are not attracted to water and may seem to be repelled by it. Hygroscopics ''are'' attracted to water, but are not dissolved by water. Molecules A hydrophilic molecule or portion of a molecule is one whose interactions with water and other polar substances are more thermodynamically favorable than their interactions with oil or other hydrophobic solvents. They are typically charge-polarized and capable of hydrogen bonding. This makes these molecules soluble not only in water but also in polar solvents. Hydrophilic molecules (and portions of molecules) can be contrasted with hydrophobic molecules (and portions of molecules). In some cases, both hydrophilic and hydrophobic properties occur in a single molecule. An example of these amphiphilic ...
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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 Protein secondary structure, 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. The alpha helix has a right-handed helix conformation in which every backbone amino, N−H group hydrogen bonds to the backbone carbonyl, C=O group of the amino acid that is four residue (biochemistry), residues earlier in the protein sequence. Other names The alpha helix is also commonly called a: * Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure) * 3.613-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen) Discovery ...
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Integral Membrane Protein
An integral, or intrinsic, membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins can be classified as IMPs, but not all IMPs are transmembrane proteins. IMPs comprise a significant fraction of the proteins encoded in an organism's genome. Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein. Such proteins can only be separated from the membranes by using detergents, nonpolar solvents, or sometimes denaturing agents. Proteins that adhere only temporarily to cellular membranes are known as peripheral membrane proteins. These proteins can either associate with integral membrane proteins, or independently insert in the lipid bilayer in several ways. Structure Three-dimensional structures of ~160 different integral membrane proteins have been determined at atomic resolution by X-ray crystallography or nucle ...
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