This document discusses the different types of bonds that contribute to tertiary protein structure. Disulfide bridges form covalent bonds between cysteine residues and significantly stabilize protein structure by holding folded chains in place. Ionic bonds can form between positively and negatively charged amino acids deep inside proteins. Hydrophobic interactions involve non-polar amino acids clustering together inside the protein core, while hydrogen bonds form between polar residues on the surface.
This document discusses the different types of bonds that contribute to tertiary protein structure. Disulfide bridges form covalent bonds between cysteine residues and significantly stabilize protein structure by holding folded chains in place. Ionic bonds can form between positively and negatively charged amino acids deep inside proteins. Hydrophobic interactions involve non-polar amino acids clustering together inside the protein core, while hydrogen bonds form between polar residues on the surface.
This document discusses the different types of bonds that contribute to tertiary protein structure. Disulfide bridges form covalent bonds between cysteine residues and significantly stabilize protein structure by holding folded chains in place. Ionic bonds can form between positively and negatively charged amino acids deep inside proteins. Hydrophobic interactions involve non-polar amino acids clustering together inside the protein core, while hydrogen bonds form between polar residues on the surface.
Disulphide Bridges - Form when 2 cysteine molecules are close together. An oxidation reaction occurs between the two sulfur-containing groups, resulting in a strong covalent bond forming which is the disulphide bond. Significantly stabilizes the structure and are important for holding the folded polypeptide chains in place.
Ionic Bonds - Form between some of the strongly
positive and negative amino acid side chains, which are sometimes found deep inside the protein molecule. - Strong bonds but not as common as structural bonds.