Proteins Flashcards
At their isoelectric point (pI), what form are amino acids in?
Their zwitterion form.
Which is the only amino acid that is not chiral around its alpha carbon?
Glycine.
Name the aliphatic and hydrophobic amino acids.
Alanine, Valine, Leucine, Isoleucine.
Which amino acid has no side chain?
Glycine.
Name the only imino acid?
Proline.
Name the positively charged amino acids?
Arginine, Lysine and Histidine.
Which of the positively charged amino acids is very basic and why?
Arginine. The positive charge is destabilised by resonance.
Which amino acids are negatively charged?
Aspartic Acid (Aspartate) and Glutamic Acid (Glutamate).
Which amino acids have polar side chains? Which one is both polar and aromatic?
Asparagine, Glutamine, Serine, Threonine, and Tyrosine. Tyrosine is both polar and aromatic.
Which amino acids have sulfur-containing side chains?
Cysteine and Methionine.
Which amino acids have non-polar aromatic side chains?
Phenylalanine and Tryptophan.
What three states can an amino acid exist in?
Cation (at low pH), zwitterion at it’s pI (approximately neutral pH) and an anion at high pH.
What is the pKa?
The centre point of the titration for each group.
Why is the pKa of the carboxyl group in amino acids higher than that for carboxylic acids?
The amino group withdraws electrons from the carboxyl group, stabilising the negatively charged form.
If the amino acid has an ionisable side chain, how many pKa values will the titration curve have?
3
Which enantiomer of amino acids is found in proteins?
L
How can you tell if an amino acid is the L enantiomer?
If you can spell CORN with H pointing towards you, reading clockwise, then it is the L enantiomer.
Why is there restricted rotation around peptide bonds?
They have partial double bond character as they are resonance hybrids.
Usually, the C=O bond and the N-H bond point in opposite directions in a peptide linkage. Why?
Otherwise there is steric clash between R groups.
What does it mean to say that polypeptides are monodisperse? Is this true for polysaccharides?
All polypeptides of the same type are the same length. No, polysaccharides are polydisperse.
What is the primary structure of a protein?
The genetically pre-determined sequence of amino acids.
What is the secondary structure of a protein?
The folding of the protein based on the non-covalent interactions between peptide bonds.
What two angles are used to define the angles of bond rotation in a peptide bond? What is their range of values?
φ and ψ
-180 to 180 degrees.
Due to steric hindrance, only some angles of rotation are possible. What plot is used to show these?
Ramachandran plot
What are the values of φ and ψ in proline?
φ = -60 degrees, ψ = -77 degrees.
Why is rotation restricted in proline?
The bond between the alpha carbon and nitrogen is part of the pyrrolidine ring.
Why does glycine allow a far wider range of angles of rotation?
It only has a H in its side chain, so there is little to no steric hindrance.
What are the criteria for the formation of a stable secondary structure?
Peptide bonds must be planar and have favourable bond lengths and angles.
Every carbonyl carbon and amide nitrogen are involved in hydrogen bonding.
The H bonded atoms are in a straight line.
Operation to move from one residue to another is always the same.
Side-chains point out of the structure for minimal steric interference.
What are the two main types of secondary structure?
Alpha-helix and beta-pleated sheet.
In an alpha helix, a peptide bond ‘i’ will form hydrogen bonds with which peptide bond?
i+4.
Which end of the alpha helix do all N-H groups in peptide bonds point towards?
The N-terminus.
For L-amino acids, what is the screw-sense of the alpha-helix?
Clockwise when looking down from the N-terminus.
Another helical form is the π helix. What peptide bonds will form hydrogen bonds?
i, i+5.
What residues are often found where there is a π helix?
Proline, due to its limited rotation.
What are the values of φ and ψ in an alpha helix?
φ = -60 degrees ψ= -45 degrees
What are the values of φ and ψ in a beta-pleated sheet?
φ = -120 degrees ψ= 120 degrees
In a beta sheet, in which directions do the carbonyl and amide groups in the peptide bond point?
They alternate directions.
Why is the anti-parallel beta sheet more stable than the parallel one?
In the anti-parallel form, the atoms making up the double bond are in a straight line. In the parallel form, this is not the case.
Which directions do the side-chains point in a beta sheet?
They alternate above and below the sheet.