Amino Acid Properties Flashcards
Which amino acid has the highest R group pKa?
Arginine, pKa of 12.5
Which group on an amino acid has the lowest pKa?
Alpha Carboxyl group
What is the pKa of the alpha amino group?
8
Proteins exclusively contain: L or D amino acid isomers
L-amino acids are only found in proteins, L and D reflect R and COO- groups
Where would a carbon labelled C-1 be on an amino acid?
This would be the carboxyl carbon, not same place as alpha-carbon which is chiral
An ion which contain both positive and negative charges ic called…
a zwitterion
A compound with a low pKa would be an acid or a base?
Acid (stronger if lower pKa)
What is the Henderson-Hasselbach equation?
pH = pKa+ log([A-]/[HA])
If the pH of a weak acid solution is greater than its pKa, what would the relative concentrations of A- and H+ be?
Conc. A- is greater than conc. HA
What is phosphorylation (in relation to proteins)?
The addition of a phosphate group to a polar, neutral amino acid in place of a hydroxyl group (affect S, T, Y -> MAPK)
What 3 amino acids may be phosphorylated?
Serine (S), Tyrosine (Y) and Threonine (T)
What is the use of phosphorylation?
Modulating protein function, cellular signalling, protein kinases
What disease is caused by a mutation in protein kinases?
Cancer (Protein kinases phosphorylate proteins)
What are the 6 Amino acids which are hydrophobic, with a non polar R group?
Glycine (G), Alanine (A), Valine (V), Leucine (L), Isoleucine (I) and Methionine (M)
Which amino acid is the most hydrophobic?
Methionine, due to methyl-thioether (methyl group bound to Sulphur)
What is the ring structure in proline known as?
Pyrrolidine Ring
Which amino acid from does proline favour?
Trans form (most Amino acids favour the cis form)
Which amino acid are aromatic?
Phenylalanine (F), Tryptophan (W), Histidine (H), Tyrosine (Y) - but Histidine does not absorb light at 280nm like others
Which amino acids contain Hydroxy groups?
Serine (S), Threonine (T), Tyrosine (Y) —> can be phosphorylated
What amino acid has a pKa very similar to physiological pH and as such is uncharged and can act as acid/base?
Histidine (H), ability to conduct acid/base chemistry makes it useful in enzymes such as carbonic anhydrase
What enzyme forms 4 disulphide bonds and is used by the body to defend against infection?
Lysozyme(s)
What amino acids are positively charged?
Lysine (K), Arginine (R) and sometimes Histidine (H) - contribute to basicity
What is the major driving force behind protein folding?
Hydrophobic character of residues
What mentioned enzyme is Histidine (H) present in?
Carbonic Anhydrase