Amino Acids (ht Only) (GCSE Chemistry)

Which statement about side chains of acidic amino acids (aspartic and glutamic acid) is true at physiological pH (~7.4)?

An amino acid contains both an amine group and a carboxylic acid group. Which of the following best describes the bond formed when two amino acids join to make a dipeptide?

At a pH below the isoelectric point (pI) of an amino acid, what is the predominant net charge on the molecule?

Which technique can distinguish L- and D- enantiomers of amino acids by measuring the rotation of plane-polarised light?

In electrophoresis of amino acids at a pH above their isoelectric point, which direction will a typical amino acid molecule migrate?

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?

Which statement about peptide bond geometry is correct?

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

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

Amino acids can act as buffers. Around which pH value does an amino acid buffer strongly?

Which analytical change would you expect when an amino acid sample is titrated, passing its isoelectric point pI?