Amino Acids (ht Only) (GCSE Chemistry)

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 statement explains why peptide bonds absorb strongly in the infrared (IR) spectrum around 1650 cm-1 (amide I band)?

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

Which amino acid side chain is basic and therefore likely to be positively charged at physiological pH?

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

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?

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?

Which reagent gives a purple (Ruhemann’s purple) colour when it reacts with free amino acids, and is used to detect amino acids in chromatography spots?

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

Which process describes the hydrolysis of a polypeptide back to its constituent amino acids?

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