CW2: Amino acid structure Flashcards
Why is rotation around a peptide bond not possible?
The peptide bond is planar due to its partial double-bond character, which limits the rotation angle between amino acids
What is the amino acid with the simplest side chain?
Glycine
What is the name and structure of the intermediate between the two forms of a peptide? Why is it unable to rotate?
Resonance hybrid
It cannot rotate due to the partial double bonds making it a planar molecule
Name the amino acids with polar, positively charged side chains and give their three- and one-letter abbreviations
Lysine / Lys / K
Arginine / Arg / R
Histidine / His / H
Between which bonds in a peptide is free rotation permitted? What is the name of the angles of these bonds, and why are certain values of these angles not permitted?
Free rotation is permitted between:
- Cα –C bond: psi (Ψ) angle
- N–Cα bond: phi (Φ) angle
Certian values aren’t permitted because of steric hindrance (side chains hitting each other).
How can serine and threonine be modified after synthesis? Explain this process if there were a lack of O2 in the cell.
Phosphorylation: adding PO32– to the amino acid
Receptor discovers lack of O2 → Cell nucleus responds with a phosphorylation reaction → Can turn off signal as well using phosphatase (i.e. it is a reversible reaction)
Why are localised pH effects very influential on histidine?
Its pK is 6.5 which is close to a pH of 7, therefore histidine can either accept or donate protins. This means that a small change in pH in either direction can cause a large change in the properties of amino acid chains containing histidine
What are the special properties of proline?
- Not very polar and not very non-polar
- Side chain is chemically linked to the backbone so not very flexible
Name the amino acids with polar, uncharged side chains and give their three- and one-letter abbreviations
Serine / Ser / S
Threonine / Thr / T
Asparagine / Asn / N
Glutamine / Gln / Q
Cysteine / Cys / C
What is the bond between two amino acids? How does it form?
Peptide bond
W
Which amino acids have hydroxyl groups and what influence does this have on their behaviour?
- Tyrosine
- Serine
- Threonine
They can be modified after synthesis (e.g. phosphorylated)
Why do we often say ‘aspartate/glutamate’ not ‘aspartic acid/glutamic acid’?
These amino acids tend to exist negatively charged (because their pKs are approx. 4.4 at pH 7, so they are less protonated (i.e. pH is higher than pK) so protons are given up), hence ‘–ate’
Name the amino acids with non-polar, aromatic side chains and give their three- and one-letter abbreviations
Phenylalanine / Phe / F
Tryptophan / Trp / W
Tyrosine / Tyr / Y
Which amino acids have sulfur in their side chains? What are the differences in their properties?
Methionine and cysteine
The sulfur in methionine is buried in the side chain so has no large bearing on its properties
Cysteine can form dislfide bonds with other amino acids becuase its sulfur is at the end of the side chain