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2ND SEM BIOCHEMISTRY > [RECALLS] Prelims - 2nd Evals > Flashcards

[RECALLS] Prelims - 2nd Evals Flashcards

1
Q

Aromatic amino acid with positive charge:

A

Histidine

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2
Q

Backbone of cysteine:

A

Serine

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3
Q

More than 10 residues:

A

Fibrous

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4
Q

Optically active B carbon:

A

Isoleucine

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5
Q

Essential for baby even though the body already produces it:

A

Arginine

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6
Q

Amino acid nucleus:

A

A-carbon

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7
Q

Rod like appearance:

A

Alpha helix

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8
Q

Coiled:

A

Alpha helix

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9
Q

Katong sa UV

A

Tryptophan

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10
Q

Cyclic

A

Proline

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11
Q

No L or D isomers:

A

Glycine

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12
Q

Represents an obligatory interruption of a helix:

A

Prolyl residue

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13
Q

Katong sa turns/folds:

A

Turns and bends

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14
Q

Secondary structure:

A

Hydrogen bonds

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15
Q

2 or more chains are united:

A

Quarternary

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16
Q

Transforms ammonium ion into a-amino nitrogen:

A

Aminotransferase

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17
Q

pKa:

A

Strengths of weak acid

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18
Q

pH>pI

A

Net charge is negative

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19
Q

Three dimensional shape

A

Tertiary structure

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20
Q

Temporary fluctuating dipoles:

A

Van der waals

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21
Q

Pyruvate to alanine

A

ALT (Alanine transaminase)

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22
Q

3rd reaction (phosphoglycerate to serine)

A

Dephosphorylation (Oxidation, transamination, dephosphorylation)

23
Q

Reaction II of tyrosine

A

Dihydrobiopterin to TETRAHYDROBIOPTERIN (Tyrosine reaction is irreversible)

*Reaction 1: L-phenylalanine to L-tyrosine by phenylalaline hydroxylase

24
Q

Most hydrophobic

A

Methionine

25
Q

Katong secondary structure na naay slant:

A

Beta parallel

26
Q

Product sa choline:

A

Betainealdehyde

27
Q

Urea cycle precursor:

A

Ornithine

28
Q

How many isoforms is formed in a chimeral structure:

A

2

29
Q

Double ring daw na amino acid:

A

Tryptophan

30
Q

Will facilitate the folding of unfolded structure:

A

Domains or region

If facilitate refolding process: Contacts and Region

31
Q

2 amino acids that interrupt in folding:

A

Proline: Large
Glycine: Small

32
Q

Angle between alpha carbon and carbonyl carbon:

A

psi -47

PHIN -57: Alpha carbon and nitrogen carbon

33
Q

Amino acid not a product in TCA:

A

Cysteine, Hydroxylysine, Tyrosine ??

34
Q

Indole

A

Tyrosine

35
Q

At physiologic pH:

A

Zero

36
Q

When both sides are ionized, capable of binding to a proton:

A

Zwitterion

37
Q

Every AA has a pH with no net charge caled pI or isoelectric point so aspartic acid = pi3

A

Zero

38
Q

Ratio greater than 10

A

Fibrous proteins: structural proteins like HAIR, FIBRIN, COLLAGEN

39
Q

Sequence of amino acids in a polypeptide chain:

A

Primary structure

40
Q

Spacing of a complete turn of amino acid residue:

A

3.6 Aminoacyl residue per turn

41
Q

The H+ bonds are evenly placed, equidistant but slant in alternate direction

A

Paralle betapleated sheet

42
Q

Presence of this amino acid represents an obligatory interruption of a helix which creates a bend

A

Proyly residue

43
Q

The whole chain folds itself into its final 3D shape:

A

Tertiary structure proteins

44
Q

Temporary fluctuating dipoles in one of these groups could induce opposite dipoles in another group on a nearby folded chain

A

Van der waals dispersion forces

45
Q

Unfolded proteins that retain a number of secondary structures that facilitate the refolding process

A

Contacts and regions

46
Q

Most transaminases generate:

A

GLU & ASP

47
Q

Provide proteins with unique structural and functional properties

A

R-groups

48
Q

Amino acids are colorless except for:

A

FWY

49
Q

Present in multiple tandem repeats:

A

Proline

50
Q

Least hydrophobic, nonpolar, aromatic a.a side chain

A

Tyrosine

51
Q

Most hydrophobic, nonpolar, aromatic a.a side chain:

A

Phenylalanine

52
Q

Arginine:

A

Guanidino group

53
Q

Imidazole functional group (Has 2 N atoms in a 5 membered unsaturated ring)

A

Histidine

54
Q

Decrease in L-dopa:

A

Parkinson’s disease

2ND SEM BIOCHEMISTRY (33 decks)

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