Information about Immunoglobulin Fold
An immunoglobulin fold is a common all-β protein fold that consists of a 2-layer sandwich of ~7 antiparallel β-strands arranged in two β-sheets.
The backbone switches repeatedly between the two β-sheets. Typically, the pattern is (N-terminal β-hairpin in sheet 1)-(β-hairpin in sheet 2)-(β-strand in sheet 1)-(C-terminal β-hairpin in sheet 2). The cross-overs between sheets form an "X", so that the N- and C-terminal hairpins are facing each other.
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Protein tertiary structure | |
|---|---|
| General | Structural domain |
| All-α folds: | Helix bundle |
| All-β folds: | Immunoglobulin fold |
| α/β folds: | TIM barrel |
| α+β folds: | Ferredoxin fold |
| Irregular folds: | Conotoxin |
β sheet (also β-pleated sheet) is the second form of regular secondary structure in proteins — the first is the alpha helix — consisting of beta strands
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β sheet (also β-pleated sheet) is the second form of regular secondary structure in proteins — the first is the alpha helix — consisting of beta strands
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In biochemistry and chemistry, the tertiary structure of a protein or any other macromolecule is its three-dimensional structure, as defined by the atomic coordinates.[1]
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Relationship to primary sequence
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A structural domain is an element of overall structure within a protein that is self-stabilizing and often folds independently of the rest of the protein chain.
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A helix bundle is a small protein fold composed of three or four alpha helices and held together by nonlocal hydrophobic interactions.
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Three-helix bundles
Three-helix bundles are among the smallest and fastest known cooperatively folding structural domains...... Click the link for more information.
TIM barrel is a conserved protein fold consisting of eight α-helices and eight parallel β-strands that alternate along the peptide backbone. The structure is named after triosephosphateisomerase, a conserved glycolytic enzyme.
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ferredoxin fold is a common α+β protein fold with a signature βαββαβ secondary structure along its backbone. Structurally, the ferredoxin fold can be regarded as a long, symmetric hairpin that is wrapped once around, so that its two terminal
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conotoxin is one of a group of neurotoxic peptides isolated from the venom of the marine cone snail, genus Conus.
Conotoxins, which are peptides consisting of 10 to 30 amino acid residues, typically have one or more disulfide bonds.
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Conotoxins, which are peptides consisting of 10 to 30 amino acid residues, typically have one or more disulfide bonds.
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secondary structure is the general three-dimensional form of local segments of biopolymers such as proteins and nucleic acids (DNA/RNA). It does not, however, describe specific atomic positions in three-dimensional space, which are considered to be tertiary structure.
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In biochemistry, quaternary structure is the arrangement of multiple folded protein molecules in a multi-subunit complex.
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Description and examples
Many proteins are actually assemblies of more than one polypeptide chain, which in the context of the larger assemblage are..... Click the link for more information.
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