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Biology uses essentially 20 amino acids for its coded protein enzymes, representing a very small subset of the structurally possible products. Since life tends to use whatever is available, an explanation is needed for why the set used is so small. [ 116 ]
Cytochrome c is a highly conserved protein across the spectrum of eukaryotic species, found in plants, animals, fungi, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), [7] makes it useful in studies of cladistics. [8] Cytochrome c has been studied for the glimpse it gives into evolutionary ...
A structural domain is an element of the protein's overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. Many domains are not unique to the protein products of one gene or one gene family but instead appear in a variety of proteins.
A scenario is a set of related concepts pertinent to the origin of life (abiogenesis), such as the iron-sulfur world. Many alternative abiogenesis scenarios have been proposed by scientists in a variety of fields from the 1950s onwards in an attempt to explain how the complex mechanisms of life could have come into existence. These include ...
A protocell is a pre-cell in abiogenesis, and was a contained system consisting of simple biologically relevant molecules like ribozymes, and encapsulated in a simple membrane structure – isolating the entity from the environment and other individuals – thought to consist of simple fatty acids, mineral structures, or rock-pore structures.
The dynamics of the elementary hypercycle can be modelled using the following differential equation: [3] ˙ = (+,) where =, =. In the equation above, x i is the concentration of template I i; x is the total concentration of all templates; k i is the excess production rate of template I i, which is a difference between formation f i by self-replication of the template and its degradation d i ...
The colloidal protein hypothesis stated that proteins were colloidal assemblies of smaller molecules. This hypothesis was disproved in the 1920s by ultracentrifugation measurements by Theodor Svedberg that showed that proteins had a well-defined, reproducible molecular weight and by electrophoretic measurements by Arne Tiselius that indicated ...
Proteoglycans are proteins [1] that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein " with one or more covalently attached glycosaminoglycan (GAG) chain(s). [ 2 ] The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate ...