Biochemistry Flashcards

1
Q

Chiral

A

AKA stereogenic center Has four different groups attached to carbon Optically active

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2
Q

Nonpolar amino acids

A

Glycine, alanine, valine, leucine, isoleucine, methionine, proline, phenylalanine, tryptophan

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3
Q

Polar amino acids

A

Tyrosine, serine, threonine, cysteine, asparagine, glutamine

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4
Q

Acidic amino acids

A

Aspartate and glutamate

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5
Q

Basic amino acids

A

Lysine, arginine, histidine

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6
Q

Catalytic triad

A

Found in chymotrypsin The histidine residue in its active site removes a proton from the -COOH group in an aspartic acid residue, which can then deprotonate a serine residue.

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7
Q

Amphoteric species

A

Can either accept a proton or donate a proton

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8
Q

pKa

A

The pH at which, on average, half of the molecules of that species are deprotonated. [HA]=[A-] If pH < pKa then majority protonated If pH > pKa then majority deprotonated

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9
Q

Amino acid deprotonation

A

pKa1 = pKa for carboxyl group = 2 pKa2 = usually amino group = 9-10

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10
Q

Zwitterions

A

At pH 7.4, you will have zwitterion COO- and NH3+ Overall charge is neutral

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11
Q

Isoelectric point (pI)

A

The pH at which the molecule is electrically neutral.

(pka1 + pKa2)/2 = pI of neutral aa

average of two lowest pKa’s for acidic aa

average of two highest pKa’s for basic aa

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12
Q

Oligopeptide

A

A relatively small peptide, up to about 20 residues

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13
Q

Peptide bond

A

Joins residues in peptides together. Forms between the COO- of one group and the NH3+ of another. Forms through dehydration or condensation reaction. Has partial double bond character from resonance.

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14
Q

Hydrolytic enzymes

A

Catalyze hydrolysis of peptides. Trypsin and chymotrypsin. Break apart amide bond by adding a hydrogen atom to the amide nitrogen and an OH group to the carbonyl carbon.

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15
Q
A
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16
Q

Lactose

17
Q

Sucrose

18
Q

Glycogen

19
Q

Starch

20
Q

Cellulose

21
Q

Secondary Structure

A

H-bonds between amino hydrogens and carboxyl oxygen atoms of backbone.

Alpha helixes and Beta sheets

22
Q

Tertiary structure

A

Interaction of side chains (hydrophobic interactions, VDW forces, ionic bonds, and H bonds)

23
Q

Competitive Inhibition

A

Inhibitor competes with substrate to bind to active site

Can be overcome by increasing the concentration of substrate

Vmax does not change

Km increases

24
Q

Noncompetitive Inhibition

A

Inhibitor binds to allosteric site that causes conformational change of active site and prevents substrate from binding. Can bind to enzyme or enzyme-substrate complex.

Km does not change

Vmax decreases

25
Uncompetitive Inhibition
Inhibitor binds to enzyme-substrate complex (can’t bind to enzyme alone) and prevents substrate from being released. Allosteric site is opened only after substrate binds to enzyme Km is lowered Vmax is lowered
26
Acetylation
Euchromatin DNA less tightly bound Chromatin is more active
27
Methylation
heterochromatin