Covalent bonds are formed by atoms with similar electronegativity, which each donate a valence electron to form a shared electron-pair bond. ... This is what makes peptide bonds planar, as atoms cannot rotate around this rigid bond. ... Another non-covalent interaction is the salt-bridge. ... A disulphide bond is created when two cysteine residues are oxidised to form a sulphur-sulphur covalent bond and is the only covalent bond formed by the side-chains of residues in a protein. Disulphide bonds are relatively strong as they are covalent, but are weak in comparison to the other covalent bonds...

• Word Count: 1582
• Approx Pages: 6
• Grade Level: Undergraduate

It is connected by peptide bonds, and the sequence determines the structure and shape of the whole protein. ... All covalent links in a protein are included in the primary structure. ... A beta pleated sheet is a form of shape where the bonds create a kinked shape, and attract across the space, as in the diagram overleaf. ... Various types of bonds are used in these links: hydrogen bonds between R groups, disulphide bonds between two cysteines molecules, as in the primary structure, ionic bonds between R groups containing amine and carboxyl groups, and hydrophobic reactions between R groups wh...

• Word Count: 467
• Approx Pages: 2
• Grade Level: High School

During the process of protein synthesis for the normal and mutated prion, special bonds known as peptide bonds form a polypeptide chain. ... The helical structure of a polypeptide results from hydrogen bonds between elements of peptide bonds that are distributed along the backbone of the chain. ... They are stabilized by hydrogen bonds between the elements of the peptide linkage. ... The intermolecular interactions are a result of hydrogen, ionic and covalent interactions. ...

• Word Count: 1313
• Approx Pages: 5