Antifungal protein

In molecular biology, proteins in the antifungal protein family consist of five antiparallel beta strands which are highly twisted creating a beta barrel stabilised by four internal disulphide bridges. ^[1]

7 relations: Antiparallel (biochemistry), Beta barrel, Beta sheet, Binding site, Hydrophobe, Ion, Phospholipid.

Antiparallel (biochemistry)

In biochemistry, two biopolymers are antiparallel if they run parallel to each other but with opposite alignments.

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Beta barrel

A beta barrel is a beta-sheet that twists and coils to form a closed structure in which the first strand is hydrogen bonded to the last.

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Beta sheet

The β-sheet (also β-pleated sheet) is a common motif of regular secondary structure in proteins.

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Binding site

In biochemistry, a binding site is a region on a protein or piece of DNA or RNA to which ligands (specific molecules and/or ions) may form a chemical bond.

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Hydrophobe

In chemistry, hydrophobicity is the physical property of a molecule (known as a hydrophobe) that is seemingly repelled from a mass of water.

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Ion

An ion is an atom or molecule that has a non-zero net electrical charge (its total number of electrons is not equal to its total number of protons).

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Phospholipid

Phospholipids are a class of lipids that are a major component of all cell membranes.

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References

[1] https://en.wikipedia.org/wiki/Antifungal_protein

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