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7 relations: Alpha helix, DSSP (hydrogen bond estimation algorithm), Lifson–Roig model, Polyproline helix, Protein secondary structure, STRIDE, 310 helix.
Alpha helix
The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a righthand-spiral conformation (i.e. helix) in which every backbone N−H group donates a hydrogen bond to the backbone C.
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DSSP (hydrogen bond estimation algorithm)
The DSSP algorithm is the standard method for assigning secondary structure to the amino acids of a protein, given the atomic-resolution coordinates of the protein.
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Lifson–Roig model
In polymer science, the Lifson–Roig model is a helix-coil transition model applied to the alpha helix-random coil transition of polypeptides; it is a refinement of the Zimm-Bragg model that recognizes that a polypeptide alpha helix is only stabilized by a hydrogen bond only once three consecutive residues have adopted the helical conformation.
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Polyproline helix
A polyproline helix is a type of protein secondary structure which occurs in proteins comprising repeating proline residues.
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Protein secondary structure
Protein secondary structure is the three dimensional form of local segments of proteins.
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STRIDE
In protein structure, STRIDE (Structural identification) is an algorithm for the assignment of protein secondary structure elements given the atomic coordinates of the protein, as defined by X-ray crystallography, protein NMR, or another protein structure determination method.
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310 helix
A 310 helix is a type of secondary structure found in proteins and polypeptides.
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