Midterm 2 Random Flashcards

1
Q

primary structure

A

what amino acids make up the structure

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2
Q

secondary structure

A

describes some aspects of 3d, h-bonding between backbone, a-helix (flexible), and beta-pleated sheets (strong)

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3
Q

tertiary structure

A

how protein folds to achieve active form (side chain int.: h-bonding, salt bridges, hydrophobic effects, disulfide bonds, pi-stacking)

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4
Q

quaternary structure

A

multiple subunits in active form (bonding motif in center of subunits)

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5
Q

denaturing a protein

A

-disrupt interactions
-change pH- h-bonding-salt bridge most affected
-chemical: THF disrupts hydrophobic most
-heat + agitation

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6
Q

Peptide bonds

A

connect the residues

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7
Q

enzymes

A

catalyze reactions lowers delta G double dagger

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8
Q

pi-stacking

A

sandwich, t-shaped, parallel-displaced

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9
Q

synthesis of amino acids

A

Strecker Synthesis:
1) NH3, trace acid
2)HCN
3) acid, D

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10
Q

heterocyclic amino acids

A

Proline, tryptophan, histidine:
confers a variety of properties, catalysis, and pi-stacking

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11
Q

Benzene Amino Acids

A

Tyrosine, Phenylalanine:
useful for hydrophobic pockets, pi-stacking, and the creation of complex biomolecules

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12
Q

Amide-based Amino Acids

A

Asparagine, glutamine
amide in side chain, increases polarity of the compound, can engage in coupling rxns and other synthetic routs

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13
Q

Basic Amino Acids

A

-amine on their side chains
-+1 charge
-heavily involved in catalysis
-histidine can act as acid or base b/c pKa value
-engages in Acid Catalysis

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14
Q

Acidic Amino acids

A

-carboxylic acid on side chain
-can engage in basic catalysis
-low pka values, usually in conj. base form increasing water solubility

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15
Q

Sulfur containing Amino acids

A

-used to create hydrophobic pockets in proteins

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16
Q

disulfide bonds

A

contains thiol functional group, can be oxidized to disulfides

17
Q

Aliphatic Amino acids

A

have a hydrophobic side chain(just c’s), useful for repelling water (hydrophobic pockets)

18
Q

Physiological pH

A

7.4!!!!

19
Q

Glyosidic Bond

A

-Monosaccharides combine to form polysaccharides

20
Q

more shielded

A

lower ppm

21
Q

more deshielded

A

higher ppm

22
Q

splitting

A

n+1 rule
ex: splits into quartet b/c 3 adjacent adjacent H that are not the same as it but same as each other

23
Q

Conformational equilibrium

A

EN atoms create their own magnetic feild , rest rapidly rotating

24
Q

Higher peaks

A

due to integral value (how many H are actually on the carbon)

25
Q

HOMOTPIC

A

same protons

26
Q

heterotopic

A

not same protons

27
Q
A