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BOARD EXAM REVIEW > Biochemistry > Flashcards

Biochemistry Flashcards

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1
Q

Protein involved in the first step of heme synthesis. Conjugates to bile acids, drugs, and other metabolites. Major inhibitory neurotransmitter in the spinal cord. Non-polar amino acid with the smallest side chain.

A

Glycine

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2
Q

Protein involved in transporting ammonia and pyruvate carbons from skeletal muscle to liver. Together with glycine, constitutes a major fraction of free amino acids in the blood.

A

Alanine

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3
Q

Accumulates in PKU, precursor of Tyrosine

A

Phenylalanine

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4
Q

Largest side chain. Precursor for niacin, serotonin, melatonin.

A

Tryptophan

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5
Q

Transfers methyl groups (SAM), and precursor of homocysteine

A

Methionine

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6
Q

Imino acid, interrupting alpha-helix structure of globular proteins. Contributes to the fibrous structure of collagen.

A

Proline

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7
Q

Branched chain amino acids that accumulate in MSUD

A

Valine, Isoleucine, Leucine

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8
Q

Contains polar hydroxyl group. O-linked glycosylation and phosphorylation of proteins.

A

Serine, Threonine, Tyrosine

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9
Q

Precursor of L-Dopamine, Dopamine, Norepinephrine, Epinephrine, Melanin, Thyroxine

A

Tyrosine

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10
Q

Contains carbonyl group and an amide group that can form hydrogen bonds

A

Glutamine, Asparagine

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11
Q

Site for N-linked glycosylation of proteins

A

Asparagine

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12
Q

Deaminated by glutaminase to form ammonia which carries nitrogen from peripheral tissues to the liver

A

Glutamine

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13
Q

Contains a sulfhydryl group. Participates in the biosynthesis of Coenzyme A (CoA). Two of which can combine by a covalent disulfide bond producing a protein complex found in keratin.

A

Cysteine

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14
Q

Acidic amino acids. Containing carboxylate group. Participate in ionic interactions, and serve as proton donors.

A

Aspartate, Glutamate

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15
Q

Precursor for GABA and glutathione

A

Glutamate

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16
Q

Basic amino acids, proton acceptors.

A

Histidine, Arginine, Lysine

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17
Q

At neutral pH, these basic amino acids are positively charged.

A

Arginine and Lysine

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18
Q

Basic amino acid with no charge

A

Histidine

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19
Q

Precursor of Histamine, released at the Hypothalamus via circadian rhythm

A

Histidine

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20
Q

Precursor of creatinine, urea, and nitric oxide

A

Arginine

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21
Q

21st amino acid where a selenium atom replaces the sulfur of the structural analog. Inserted into polypeptides during translation but is not specified by a simple 3-letter codon

A

Selenocysteine

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22
Q

Plant L-alpha-amino acid present in Lathyrus seeds, implicated in neurolathyrism (progressive, irreversible, spastic paralysis of lower extremities)

A

Homoarginine and B-N-Oxalyldiaminopriopionic acid (B-ODAP)

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23
Q

Plant L-amino acid, neurotoxic found in Cycad seeds. Implicated in Amyotropic Lateral Sclerosis in natives of Guam

*BONUS: other name for ALS

A

B-methylaminoalanine

BONUS: Lou-Gherig’s disease

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24
Q

All amino acids are chiral except for?

A

Glycine

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25
Q

Protein configuration

A

L-configuration

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26
Q

Bacterial Cell Wall protein configuration

A

D-configurations

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27
Q

An amino acid with no net charge

A

Zwitterion

28
Q

Essential Amino Acids

A 
Phenylalanine
Valine
Tryptophan
Threonine
Isoleucine
Methionine
Histidine
Arginine
Lysine
Leucine
29
Q

Nutritionally SEMIessential amino acid

A

Arginine

30
Q

Amino acids synthesized in the body but only from precursors

A

Cystine, Tyrosine

31
Q

Protein structure determined by SEQUENCE.

A

Primary structure

32
Q

Partial double-bond character, rigid and planar, generally in TRANS configuration. Disrupted by hydrolysis through prolonged exposure to a strong acid/base at elevated temperature

A

Peptide Bonds

33
Q

Stepwise process of identifying the specific amino acid at each position in the peptide chain

A

Sequencing

34
Q

1-fluoro-2,4-dinitrobenzene

A

Sanger’s Reagent

35
Q

Phenylisothiocyanate

A

Edman’s Reagent

36
Q

Folding of short 3-30 residue contiguous segments of polypeptide into geometrically-ordered units, stabilized by hydrogen bonding

A

Secondary structure

37
Q

Spiral structure with polypeptide backbone core with side chains extending outward, 3.6 AA per turn, disrupted by proline, or AAs with large/charged groups

A

Alpha helix

38
Q

Supersecondary structures produced by packing side chains from adjacent secondary structural elements close to each other

A

Motifs

39
Q

Specialized group of proteins required for the proper folding of many species of proteins. Prevents aggregation.

A

Chaperones

40
Q

Results in the unfolding and disorganization of the protein’s secondary and tertiary structures. NOT accompanied by the hydrolysis of peptide bonds.

A

Denaturation

41
Q

Fatal, neurodegenerative diseases characterized by spngiform changes, astrocytic gliomas, and neuronal loss resulting from the deposition of insiluble protein aggregates in neural cells.

A

Prion Diseases

42
Q

Enzyme involved in the rate-limiting step of converting Acetyl CoA to Malonyl CoA in Lipogenesis

A

Acetyl CoA carboxylase

43
Q

Sequence of steps in elongation of lipids, repeated seven times

A

Condensation, Reduction, Dehydration, Reduction

44
Q

Where do fatty acids undergo further elongation?

A

Endoplasmic Reticulum

45
Q

Up to which “carbon” can desaturation of fatty acids occur in the Endoplasmic Reticulum?

A

Carbon 9

46
Q

Apart from producing NADH for fatty acid synthesis, where can you find the enzyme isocitrate dehydrogenase?

A

Conversion of isocitrate to alpha-ketoglutarate in the TCA cycle

47
Q

What coenzyme does carboxylase use?

A

Biotin

48
Q

How are TAGs synthesized?

A

Addition of 2 fatty acyl CoA to glycerol-3-phosphate
Removal of phosphate
Addition of 3rd fatty acyl CoA

Kaya TRIacylglycerol

49
Q

In Beta Oxidation of Lipids/Fatty Acids, what is the rate-limiting step?

A

Translocation of fatty acyl CoA from the cytosol to the mitochondria

50
Q

Enzyme used in translocation of fatty acyl CoA from the cytosol to the mitochondria

A

Carnitine-palmitoyl transferase

51
Q

What are the products of Beta-Oxidation? (Acetyl CoA, NADH, FADH)

A

8 Acetyl Coa, 7 NADH, 7 FADH

52
Q

Where does Beta-Oxidation of Fatty Acids occur?

A

Mitochondria

53
Q

Where does carnitine acyltransferase-1 attach fatty acyl to carnitine?

A

Outer mitochondrial membrane

54
Q

Where does carnitine acyltransferase-2 attach fatty acyl to acyl CoA?

A

Mitochondrial matrix

55
Q

Degradation of Fatty Acyl CoA steps repeated 7 times

A

Oxidation, Hydration, Oxidation, Thiolysis

56
Q

Products of the degradation of Fatty Acyl CoA

A

FADH2, NADH, Acetyl CoA

57
Q

Why can’t the liver use ketones as fuel?

A

Because it lacks succinyl CoA acetoacetate-CoA transferase (thiophorase)

58
Q

Main Apoprotein mediating the secretion of VLDL

A

Apo-B 100

59
Q

Main apoprotein mediating the secretion of chylomicrons

A

Apo B-48

60
Q

Apoprotein cofactor of lipoprotein lipase

A

Apo C-II

61
Q

Apoprotein mediating uptake of chylomicron remnants and IDLs

A

Apo-E

62
Q

Hyperlipoproteinemia causing thrombosis due to inhibition of fibrinolysis

A

Familial Lipoprotein (a) Excess

63
Q

Hyperlipoproteinemia not associated with increased risk of coronary disease

A

Type I Familial Lipoprotein Lipase Deficiency

64
Q

Hyperlipoproteinemia beneficial to health and longevity

A

Familial hyperalpha-lipoproteinemia (High HDL)

65
Q

Hypolipoproteinemia caused by a defect in the loading of Apo-B with lipid (no chylomicrons or VLDL).

BONUS: How do you treat this?

A

Abetalipoproteinemia.

Treated with large doses of fat-soluble vitamins, particularly Vitamin E

66
Q

Hypoprotenemia causing Tangier Disease, Fish-eye disease, and Apo-A1 Deficiency

A

Familial-alpha lipoprotein deficiency

BOARD EXAM REVIEW (2 decks)

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