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A protein with the sequence below forms an alpha-helix. How many turns are made in the...

A protein with the sequence below forms an alpha-helix.

How many turns are made in the helix?

Explain why the properties of the amino acids in this helix result in an amphipathic protein. How might this amphipathic alpha-helix associate with the membrane?

Leu-Lys-Arg-Ile-Val-Asp-Thr-Ile-Leu-Ser-Arg-Leu-Phe-Lys

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Answer #1

. How many turns are made in the helix?

Number of amino acids = 14 (Leu-Lys-Arg-Ile-Val-Asp-Thr-Ile-Leu-Ser-Arg-Leu-Phe-Lys)

Number of amino acids in a turn = 3.6 (Alpha-helix have 3.6 amino acid residues/turn)

I.e, 14 ÷ 3.6 = 3.8888

4 turns

​​​​​​. Explain why the properties of the amino acids in this helix result in an amphipathic protein.

The amphipathic alpha helix is an secondary structural motif in biologically active peptides or proteins and it is an alpha helix with facing or opposite nonpolar and polar ends, that are oriented along the long helical axis.

Lysine (Lys) , tyrosine (Tyr) , methionine (Met) and tryptophan (Trp) are amphipathic amino acids. Here, lysine is the only amino acid that contain both polar and nonpolar ends. Leucine (Leu), isoleucine (Ile), valine (Val) and phenylalanine (Phe) are hydrophobic (contain nonpolar ends) amino acids. And arginine (Arg), Aspartic acid (Asp), threonine (Thr) and serine (Ser) are hydrophilic (contain polar ends) amino acids.

3 Leu, 2 Ile, 1 Val and 1 Phe contributes total of 7 hydrophobic amino acids. 2 Arg, 1 Asp, 1 Thr and 1 Ser contributes the total of 5 hydrophobic amino acids. And the 2 Lys contributes 2 amphipathic amino acids in the protein chain. And therefore, each amino acids in the 14 amino acid containg chain contributes the amphipathic nature of protein.

​​​​​​. How might this amphipathic alpha-helix associate with the membrane?

The alpha helix, membrane proteins are amphipathic macromolecules with a central hydrophobic segment and two flanking hydrophilic moieties, and due the presence of these large hydrophobic surfaces, these membrane macromolecules are normally located in membrane bilayers comprised of amphipathic lipids.

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