Proteins and their Building Blocks Flashcards
Protein structure is categorised into 4 levels…
Primary
Secondary
Tertiary
Quaternary
The linear sequence of amino acids determines the…
Properties of proteins
A molecule with charges, but no net charge is known as a…
Zwitterion
Peptide bonds join the terminal carbon of one amino acid to the…
N terminus (nitrogen) of another
Most amino acids are stereoisomeric, coming in a L or D forms. Proteins only contain the ? form
L for “living”
Peptide bonds are rigid due to a the formation of a… 🔒
Partial double bond
The CORN law states the order of the functional groups in L-form amino acids, assuming the hydrogen is…
Facing towards us
Chloramphenicol is an antibiotic, which works by mimicking the shape of a ? This enables it to bind to and thus inhibit the bacterial ribosome.
Peptide bond
Optical isomerism is important in the context of drug discovery and production because…
Different isomers can have very different effects
The ‘small’ amino acids are (5):
- Glycine
- Alanine
- Serine
- Threonine
- Cysteine
The charged/polar amino acids are (7):
Negatively charged: ➖ Aspartate ➖ Glutamate Polar: • Asparagine • Glutamine
Positively charged:
➕ Lysine
➕ Arginine
➕ Histidine
The hydrophobic amino acids are (4): 💧🙅♂️
- Valine
- Leucine / Isoleucine
- Methionine
- Proline
The aromatic amino acids are (3):
- Phenylalanine
- Tyrosine
- Tryptophan
The aromatic amino acids are also…
Hydrophobic
The largest amino acids are the…
Aromatic amino acids
Proline is notable because it…
Does not form a peptide bond
Glycine is notable for its…
Lack of optical isomerism
there are 2 hydrogens, thus the central carbon is not chiral
Phenylketoneuria is a disorder in which the body is unable to breakdown excess…
Phenylalanine
Disulphide bonds can form either between amino acid side groups or between side group and…
Metals
Disulphide bonds are only found between the thiol side groups (S/H) of which amino acids?
Cystines
Disulphide bonds increase the stability of proteins. This is particularly important for…
Extra-cellular proteins, such as pepsin, insulin or bee venom
Disulphide bonds are present in ( all / the majority / a few / no ) proteins…
A few
Each amino acid in a peptide is known as a…
Residue
Secondary structure is determined by…
Hydrogen bonds
In the alpha helix, hydrogen bonds form between peptide bonds further down the chain. The resulting helix structure has ? residues per turn
3.6
The beta sheet has two forms, X and Y. Y is less stable…
X: Antiparallel
Y: Parallel (less stable)
In the beta sheet, bonds form…
Between strands
In the beta sheet, side chains alternate…
Between up and down positions
