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17. Which type of interactions (forces) found in proteins is MOST APPROPRIATELY matched with the feature that follows? a. Ion
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a) Alpha helix secondary structure peptide chains coiled into a right handed spiral and these are stabilized by hydrogen bonds between NH and CO group.

b) The quaternary structure of protein is actually the association of many subunits into a closely packed arrangement. and each subunits has its own primary, secondary and tertiary structure. These subunits are held together by hydrogen bonds and vanderwall forces between nonpolar side chaiins.

c) The tertiary structure of a protein consists of polypeptide which is formed of a complex molecular shape. This is caused by interactions like hydrophobic, hydrophillic interactions, ionic and hydrogen bonds and also by disulohide bridges.

d) Covalent crosslinks between polypeptides is an interaction between the molecules by covalent bond as the name suggests. Attachment between groups on two different proteins results in intermolecular crosslinks that stabilize a protein protein interaction through covalent bond (peptide bond).

e) In a beta pleated sheet, the segments of polypeptide chain line up next to each other which helps to form a sheet like structure that are held by hydrogen bonds.

So, the most appropriately matched interaction is (c) that is hydrophobic interaction in tertiary structure.

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