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Tertiary in Biological Definition

Alcohol

... 1 Structure 1.1 Primary, Secondary, and tertiary Alcohols 1.2 Methanol and ethanol 2 ... pm ) in length. Primary, Secondary, and tertiary Alcohols There are three major subsets of ... is isopropanol (propan-2-ol), and a simple tertiary alcohol is tert - butanol ....

Amine

... with three carbon based groups, then it is a tertiary amine . Note: the subscripts on the R groups ... Primary Amine: Secondary Amine: tertiary Amine: Contents ... halogen acid. If the reacting amine is a tertiary amine in such a reaction, then a positive ...

Primary structure

... person either to deduce this shape (known as the tertiary structure ) or to predict localized structuring, ... Protein family ) can competely identify the tertiary structure of the given sequence. Sequence ... protein sequencing secondary structure tertiary structure quaternary structure ...

Protein

... present in one single protein molecule. tertiary structure : the overall shape of a single ... context of these functional rearrangements, these tertiary or quaternary structures are usually referred to ... are held together by hydrogen bonds . The tertiary structure is held together primarily by ...

Tertiary structure

... In biochemistry , the tertiary structure of a protein is its overall shape. ... able to perform their biological function. The tertiary structure that a protein assumes to carry out its ... the native conformation . A protein assumes tertiary structure by " folding ". An important type of ...

Gel electrophoresis

... shapes and migrate through the gel in a complicated manner based on their tertiary structure. Therefore, agents that disrupt the hydrogen bonds , such as ... proteins act like they were long rods instead of having a complex tertiary shape, the rate at which the resulting SDS coated proteins migrate in the ...

Gel electrophoresis

... shapes and migrate through the gel in a complicated manner based on their tertiary structure. Therefore, agents that disrupt the hydrogen bonds , such as ... proteins act like they were long rods instead of having a complex tertiary shape, the rate at which the resulting SDS coated proteins migrate in the ...

Quaternary structure

... the larger assemblage are known as protein subunits . In addition to the tertiary structure of the subunits, multiple-subunit proteins possess a ... complexes. See also : primary structure -- secondary structure -- tertiary structure -- structural biology -- translation ...

Secondary structure

... in three-dimensional space; the actual positions are considered to be tertiary structure. Contents showTocToggle("show","hide") 1 ... in analysis of RNA. See also : primary structure — tertiary structure — quaternary structure — translation — ...

Structural biology

... are able to perform their functions. This shape, which is called the " tertiary structure " of a molecule, depends in a complicated way on the molecule's ... prediction . See also: primary structure , secondary structure , tertiary structure , quaternary structure , structural domain , structural motif ...

Alpha helix

... elements in proteins, together with beta sheets . The peptide backbone of an α helix has 3.6 amino acids per turn. See also : tertiary structure -- β sheet -- collagen helix References David Eisenberg, "The discovery of the α-helix and β-sheet, the ...

Amino acid

... can join together by a disulfide bond to form the amino acid cystine . When cysteines are part of a protein, insulin for example, this enforces tertiary structure. D Asp Aspartic acid acidic 133.10 2.85 1.99 9.90 3.90 E Glu Glutamic acid acidic ...

Beta sheet

... sheet, when traced along the backbone, take a hairpin turn in orientation (direction), sometimes through one or more prolines . See also : tertiary structure -- α helix -- collagen helix ...

Bioinformatics

... for it. But, the protein can only function correctly if it is folded in a very special and individual way (if it has the correct secondary , tertiary and quaternary structure). The prediction of this folding just by looking at the amino acid sequence is quite difficult. Several methods for ...

Bioinformatics

... for it. But, the protein can only function correctly if it is folded in a very special and individual way (if it has the correct secondary , tertiary and quaternary structure). The prediction of this folding just by looking at the amino acid sequence is quite difficult. Several methods for ...

Disulfide bond

... is the sulfhydryl group (- S H ). Oxidation of the thiol group yields a disulfide (S-S) bond. The presence of S-S then helps to maintain the tertiary structure of the protein. An amino acid that commonly forms S-S bonds in proteins in cysteine . When two cysteines are bonded by an S-S bond, the ...

Endoplasmic reticulum

... Glycosylation involves the attachment of oligosaccharides . Disulfide bond formation and rearrangement. Disulfide bonds stabilize the tertiary and quaternary structure of many proteins. Sarcoplasmic reticulum. The endoplasmic reticulum found in muscle fibers is called sarcoplasmic ...

Ethyl alcohol

... solvent. To produce absolute ethanol, a small amount of benzene is added, and the mixture is again fractionally distilled. Benzene forms a tertiary azeotrope with water and ethanol to remove the last of the water, and a binary azeotrope with ethanol removes most of the benzene. The resulting ...

Liver

... cava. In the widely used Couinaud or "French" system, the functional lobes are further divided into a total of eight segments based on secondary and tertiary branching of the blood supply. The segments corresponding to the surface anatomical lobes are as follows: Lobe Couinaud segments ...

Molecular biology

... bacterial or eukaryotic cell. The protein can be tested for enzymatic activity under a variety of situations, the protein may be crystallized so its tertiary structure can be studied, or, in the pharmaceutical industry, the activity of new drugs against the protein can be studied. Polymerase chain ...

Protein biosynthesis

... and post-translational modification . During and after synthesis, polypeptide chains often fold to assume, so called, native secondary and tertiary structures . This is known as protein folding . Many proteins undergo post-translational modification . This is may include the formation of ...

Endoplasmic reticulum

... Glycosylation involves the attachment of oligosaccharides . Disulfide bond formation and rearrangement. Disulfide bonds stabilize the tertiary and quaternary structure of many proteins. Sarcoplasmic reticulum. The endoplasmic reticulum found in muscle fibers is called sarcoplasmic ...

Endoplasmic reticulum

... Glycosylation involves the attachment of oligosaccharides . Disulfide bond formation and rearrangement. Disulfide bonds stabilize the tertiary and quaternary structure of many proteins. Sarcoplasmic reticulum. The endoplasmic reticulum found in muscle fibers is called sarcoplasmic ...

Endoplasmic reticulum

... Glycosylation involves the attachment of oligosaccharides . Disulfide bond formation and rearrangement. Disulfide bonds stabilize the tertiary and quaternary structure of many proteins. Sarcoplasmic reticulum. The endoplasmic reticulum found in muscle fibers is called sarcoplasmic ...
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