In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest.
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In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest.
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Concept of the Protein domain was first proposed in 1973 by Wetlaufer after X-raycrystallographic studies of hen lysozyme and papainand by limited proteolysis studies of immunoglobulins.
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Each definition is valid and will often overlap, i e a compact structural domain that is found amongst diverse proteins is likely to fold independently within its structural environment.
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Domains are the fundamental units of tertiary structure, each Protein domain containing an individual hydrophobic core built from secondary structural units connected by loop regions.
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The packing of the polypeptide is usually much tighter in the interior than the exterior of the Protein domain producing a solid-like core and a fluid-like surface.
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In domain swapping, a secondary or tertiary element of a monomeric protein is replaced by the same element of another protein.
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The kinesin motor Protein domain can be at either end of a polypeptide chain that includes a coiled-coil region and a cargo Protein domain.
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Since a domain can be inserted into another, there should always be at least one continuous domain in a multidomain protein.
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Organisation of large proteins by structural domains represents an advantage for protein folding, with each domain being able to individually fold, accelerating the folding process and reducing a potentially large combination of residue interactions.
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Furthermore, given the observed random distribution of hydrophobic residues in proteins, domain formation appears to be the optimal solution for a large protein to bury its hydrophobic residues while keeping the hydrophilic residues at the surface.
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Automatic procedures for reliable domain assignment is essential for the generation of the domain databases, especially as the number of known protein structures is increasing.
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The fact that there is no standard definition of what a Protein domain really is has meant that Protein domain assignments have varied enormously, with each researcher using a unique set of criteria.
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Structural domain is a compact, globular sub-structure with more interactions within it than with the rest of the protein.
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Therefore, a structural Protein domain can be determined by two visual characteristics: its compactness and its extent of isolation.
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