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The first proteins would have had to arise without a fully-fledged system of protein biosynthesis. As discussed above, numerous mechanisms for the prebiotic synthesis of polypeptides exist. However, these random sequence peptides would not have likely had biological function.
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 ...
With microsomes there, cell-free protein synthesis demonstrates cotranslational transport of the protein into the microsome and therefore the removal of the signal sequence. This process produces a mature protein chain. Studies have looked into the cell-free protein synthesis process when microsomes have their bound ribosomes stripped away from ...
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 supersecondary structure is a compact three-dimensional protein structure of several adjacent elements of a secondary structure that is smaller than a protein domain or a subunit. Supersecondary structures can act as nucleations in the process of protein folding.
[2] [3] [4] Cytoplasmic domains collide with the actin-based membrane skeleton which induces temporary confinement or corralling of transmembrane (TM) proteins in the membrane skeleton mesh. [ 5 ] [ 6 ] TM proteins are capable to hop between adjacent compartments when the distance between the meshwork and the membrane becomes large enough, or ...
For protein sequence spaces, each residue in the protein is represented by a dimension with 20 possible positions along that axis corresponding to the possible amino acids. [3] [4] Hence there are 400 possible dipeptides arranged in a 20x20 space but that expands to 10 130 for even a small protein of 100 amino acids arranged in a space with 100 ...
Levinthal's paradox is a thought experiment in the field of computational protein structure prediction; protein folding seeks a stable energy configuration. An algorithmic search through all possible conformations to identify the minimum energy configuration (the native state) would take an immense duration; however in reality protein folding happens very quickly, even in the case of the most ...