The coiled or folded chain of amino acids is often coiled and folded further. More bonds form between different parts of the polypeptide chain
ionic bonds
attractions between negatively-charged R groups and positively-charged R groups on different parts of the molecule
disulfide bonds whenever two molecules of the amino acid cysteine come close together, the sulfur atom in one cysteine bonds to the sulfur in the other cysteine, forming a disulfide bond
Hydrophobic and hydrophilic interactions
when hydrophobic (water-repelling) R groups are close together in the protein, they tend to clump together. This means that hydrophilic (water-attracting) R groups are more likely to be pushed to the outside, which affects how the protein folds up into its final structure
hydrogen bonds
these weak bonds form between slightly positively-charged hydrogen atoms in some R groups and slightly negatively-charged atoms in other R groups on the polypeptide chain
a disulfide bond
A) disulfide bond
a proteins tertiary structure
A) hydrophilic
B) hydrogen bond
C) ionic bond
D) hydrophobic
E) disulfide bond
For proteins made from a single polypeptide chain, the tertiary structure forms their final 3D structure.
