Lecture 1 Flashcards Preview

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Flashcards in Lecture 1 Deck (41):
1

Simple building blocks

AAs, nucleotides, carbohydrates, acetate

2

Biological macromolecules

Proteins, DNA/RNA, Polysaccharides, Lipids

3

Side chain determines

Protein structure/function, electrical charge of protein

4

Side chain properties use

Methods for analysis, purification, identification

5

Aliphatic

Uncharged

6

Non-polar aliphatic

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

7

Non-polar Aromatic

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

8

Uncharged polar

Thr, Ser, Asn, Gln

9

Acidic AA

Asp, Glu - hydrophilic usually on protein/water interface

10

Basic AA

His, Lys, Arg, Strongly polar, on exterior

11

Sulfur containing AA

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

12

Proline

Constrained, aliphatic R, comparable to aliphatic AAs

13

Homocysteinuria

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.

14

Marfan's Syndrome

Associated with lens dislocation due to fibrillin gene mutations

15

Optic AAs

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

16

L

Levorotatory

17

D

Dextrorotatory

18

Amphoteric *amend this*

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

19

Zwitterion

Dipolar molecule

20

Henderson Hasselbalch eq.

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

21

Peptide bonds

loss of water (kickout of -OH of carboxyl)

22

Oligopeptides

3-10 aas

23

Polypeptides

11-99 AAs

24

Proteins (length)

100+ AAs

25

Glutathione GSH

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

y-glutamyl transpeptidase

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

27

Contributers to tertiary structure

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

28

Heme oxygenase *amend this*

Converts heme to biliverdin by removing Iron

29

Hyperbilirubin *amend this*

Green in teeth due to high bilirubin concentration

30

Ricin

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

31

Ricin A group

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

32

Barlay

A group, no B group (RICIN)

33

Chimeric Toxins

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

34

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.

35

KDEL **amend**

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

36

Essential AAs **amend**

https://quizlet.com/2855398/flashcards

37

Non-essential AAs **amend**

https://quizlet.com/2855398/flashcards

38

Amino Acids **amend**

https://quizlet.com/2855398/flashcards

39

Heme oxygenase Inhibitor

Starves bacteria of iron

40

Biliverdin

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

41

Deglycosylation

Breakdown of carbs