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Biochem 6200 > Lecture 1 > Flashcards

Lecture 1 Flashcards

1
Q

Simple building blocks

A

AAs, nucleotides, carbohydrates, acetate

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2
Q

Biological macromolecules

A

Proteins, DNA/RNA, Polysaccharides, Lipids

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3
Q

Side chain determines

A

Protein structure/function, electrical charge of protein

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4
Q

Side chain properties use

A

Methods for analysis, purification, identification

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5
Q

Aliphatic

A

Uncharged

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6
Q

Non-polar aliphatic

A

Gly, Ala, Val, Leu, Ile (from less hydrophobic to more hydrophobic)

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7
Q

Non-polar Aromatic

A

Phe, Tyr, Trp - Tyrosine and Trp hydrophobicity tempered by polar groups in side chains - help ID protein by UV

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8
Q

Uncharged polar

A

Thr, Ser, Asn, Gln

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9
Q

Acidic AA

A

Asp, Glu - hydrophilic usually on protein/water interface

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10
Q

Basic AA

A

His, Lys, Arg, Strongly polar, on exterior

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11
Q

Sulfur containing AA

A

Cys, Met, more hydrophilic than analogs, however Met is still quite hydrophobic. - Disulfide bonds

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12
Q

Proline

A

Constrained, aliphatic R, comparable to aliphatic AAs

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13
Q

Homocysteinuria

A

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.

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14
Q

Marfan’s Syndrome

A

Associated with lens dislocation due to fibrillin gene mutations

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15
Q

Optic AAs

A

All but Glycine, L (ours) and D (bacterial cell walls, peptide antibiotics).

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16
Q

L

A

Levorotatory

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17
Q

D

A

Dextrorotatory

18
Q

Amphoteric amend this

A

change charge at different pH - in aq. soln, alpha carboxyl is -, alpha amine is +

19
Q

Zwitterion

A

Dipolar molecule

20
Q

Henderson Hasselbalch eq.

A

Used for isoelectric point pH = pKa + log([CB]/[WA])

21
Q

Peptide bonds

A

loss of water (kickout of -OH of carboxyl)

22
Q

Oligopeptides

A

3-10 aas

23
Q

Polypeptides

A

11-99 AAs

24
Q

Proteins (length)

A

100+ AAs

25
Q

Glutathione GSH

A

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

26
Q

y-glutamyl transpeptidase

A

Involved in metabolism of GSH. Is a plasma biomarker for some liver diseases including hepatocellular carcinoma and alcohol disease.

27
Q

Contributers to tertiary structure

A
  1. Disulfide bonds 2. H-bonds 3. Salt Bridges 4. Hydrophobic interactions
28
Q

Heme oxygenase amend this

A

Converts heme to biliverdin by removing Iron

29
Q

Hyperbilirubin amend this

A

Green in teeth due to high bilirubin concentration

30
Q

Ricin

A

Toxic A group, binding B group (links to cells, allows entrance for A), linked by disulfide bond

31
Q

Ricin A group

A

RIP - ribosomal inactivation protein, inhibits protein synthesis. Much less toxic without B group.

32
Q

Barlay

A

A group, no B group (RICIN)

33
Q

Chimeric Toxins

A

Conjugation of A-chain of ricin to antibody to kill specific cells

34
Q

Bioengineering Ricin production amend

A

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.

35
Q

KDEL amend

A

endoplasmic reticulum ER lumen retention signal - can increase toxicity of Ricin.

36
Q

Essential AAs amend

A

https://quizlet.com/2855398/flashcards

37
Q

Non-essential AAs amend

A

https://quizlet.com/2855398/flashcards

38
Q

Amino Acids amend

A

https://quizlet.com/2855398/flashcards

39
Q

Heme oxygenase Inhibitor

A

Starves bacteria of iron

40
Q

Biliverdin

A

Product of heme and heme oxygenase - why bruises can be green.

41
Q

Deglycosylation

A

Breakdown of carbs

Biochem 6200 (18 decks)

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