Flashcards in Lecture 1 Deck (41):
Simple building blocks
AAs, nucleotides, carbohydrates, acetate
Proteins, DNA/RNA, Polysaccharides, Lipids
Side chain determines
Protein structure/function, electrical charge of protein
Side chain properties use
Methods for analysis, purification, identification
Gly, Ala, Val, Leu, Ile (from less hydrophobic to more hydrophobic)
Phe, Tyr, Trp - Tyrosine and Trp hydrophobicity tempered by polar groups in side chains - help ID protein by UV
Thr, Ser, Asn, Gln
Asp, Glu - hydrophilic usually on protein/water interface
His, Lys, Arg, Strongly polar, on exterior
Sulfur containing AA
Cys, Met, more hydrophilic than analogs, however Met is still quite hydrophobic. - Disulfide bonds
Constrained, aliphatic R, comparable to aliphatic AAs
1 in 350,000. Causes lens dislocation around age 10. Fibrillin is rich in Cysteine and thus disulfide bonds that stabilize and crosslink. Sulfite oxidase deficiency also associated with lens dislocation.
Associated with lens dislocation due to fibrillin gene mutations
All but Glycine, L (ours) and D (bacterial cell walls, peptide antibiotics).
Amphoteric *amend this*
change charge at different pH - in aq. soln, alpha carboxyl is -, alpha amine is +
Henderson Hasselbalch eq.
Used for isoelectric point pH = pKa + log([CB]/[WA])
loss of water (kickout of -OH of carboxyl)
tripeptide that forms GSSG if thiol is oxidized. Operates to maintain cysteine residues in proteins and as an antioxidant in parts of body - namely liver
Involved in metabolism of GSH. Is a plasma biomarker for some liver diseases including hepatocellular carcinoma and alcohol disease.
Contributers to tertiary structure
1. Disulfide bonds 2. H-bonds 3. Salt Bridges 4. Hydrophobic interactions
Heme oxygenase *amend this*
Converts heme to biliverdin by removing Iron
Hyperbilirubin *amend this*
Green in teeth due to high bilirubin concentration
Toxic A group, binding B group (links to cells, allows entrance for A), linked by disulfide bond
Ricin A group
RIP - ribosomal inactivation protein, inhibits protein synthesis. Much less toxic without B group.
A group, no B group (RICIN)
Conjugation of A-chain of ricin to antibody to kill specific cells
Bioengineering Ricin production **amend**
Modify E. Coli to produce A and B, which recombine to form toxin ***toxicity can be increased by deglycosylation to prevent removal from circulation by liver.
endoplasmic reticulum ER lumen retention signal - can increase toxicity of Ricin.
Essential AAs **amend**
Non-essential AAs **amend**
Amino Acids **amend**
Heme oxygenase Inhibitor
Starves bacteria of iron
Product of heme and heme oxygenase - why bruises can be green.