Amino Acids (ht Only) (GCSE Chemistry)

Which technique separates amino acids based on their differing affinities for stationary and mobile phases and can provide Rf values for identification?

What name is given to the form of an amino acid that carries both a positive and a negative charge on different atoms at physiological pH?

Which side chain property would make an amino acid more likely to be found in the interior of a folded protein (away from water)?

Which property of amino acids allows them to act as both acids and bases (amphoteric behaviour)?

Which statement correctly explains why most amino acids (except glycine) are chiral?

Which of these amino acid side chains can form a covalent disulfide bond stabilising protein tertiary structure?

During Edman degradation the N-terminal amino acid of a polypeptide is sequentially removed for identification. Which functional group does Edman chemistry target for cleavage?

Which feature distinguishes a primary, secondary, tertiary and quaternary protein structure?

A peptide has the sequence Ala–Gly–Ser. After complete hydrolysis, how many molecules of water were consumed per peptide bond broken and how many amino acids result?

Proline has a distinct structure among standard amino acids. What effect does proline commonly have on protein secondary structure?

Peptide sequencing by mass spectrometry often uses enzymatic digestion (e.g., trypsin). What is the role of trypsin in protein analysis?