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PHARM 113 > CHEMISTRY OF AMINO ACIDS > Flashcards

CHEMISTRY OF AMINO ACIDS Flashcards

1
Q

Around pH, Carboxyllic acid will be

A

Ionized (-)

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2
Q

Around pH 7, Amine group will

A

Be Ionized (+)

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3
Q

Ionized are easily dissolved in H2O

A

True

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4
Q

Solid amino acid has (MP)

A

Higher melting point

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5
Q

Alliphatic Side Chains

A

Gly, Ala, Val, Pro, Ile, Leu, Met

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6
Q

High Hydrophathy Index

A

Hydrophobic

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7
Q

Low Hydrophathy Index

A

Hydrophillic

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8
Q

Aromatic side chain

A

Phe, Tyr, His, Trp

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9
Q

Polar Uncharged side chain

A

Ser, Thr, Cys, Asn, Gln, Tyr

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10
Q

Negative charged polar side chain

A

Asp, Glu

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11
Q

Positive charged polar side chain

A

Arg, Lys, His

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12
Q

Essential amino acids

A

Source from diet

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13
Q

Non essential amino acid

A

Can be synthesize by the body

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14
Q

Separation of Amino Acids

A

Electrophoresis, and Chromatography

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15
Q

High pI

A

Cathode -

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16
Q

Low pI

A

Anode +

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17
Q

Stationary phase

A

Polar

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18
Q

Mobile phase

A

Nonpolar

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19
Q

PVTTIMHALL

A

Phe, Val, Thr, Trp, Ile, Met, His, Arg, Leu, Lys

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20
Q

L-Cysteine has

A

R configuration

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21
Q

Functions of Proteins

A

Catalytic, Contractile, Hormonal, Protective, Receptors, Regulatory, Structural, Transport

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22
Q

Catalytic

A

Enzymes

23
Q

Contractile

A

Actin, Myosin

24
Q

Hormonal

A

Insulin, hCG

25
Q

Protective

A

Fibrin, Immunoglobulins, Interferons

26
Q

Receptors

A

Nicotinic and adreganic recpetors

27
Q

Regulatory

A

Calmoudin, transcription factors

28
Q

Structural

A

Elastin, Keratin, Collagen

29
Q

Transport

A

Hemoglobin, Lipoproteins, Transferrin

30
Q

Primary structure

A

Joined by peptide bond

31
Q

Trans conformer of amino acids is

A

The most common

32
Q

Secondary structure

A

Ordered structure adopted by the chain through h bonds

33
Q

Types of secondary structures

A

Alpha helix, beta sheet, and beta turn

34
Q

Beta turn

A

4 consecutive amino acids, mostly proline and glycine, some are asparagine and aspartate

35
Q

Supersecondary structure

A

Higher than secondary but has no functions

36
Q

Forces stabilizing folding

A

Covalent, ionic, h bond, van der waals

37
Q

Chaperones

A

Involves in degradation and folding of proteins

38
Q

Prions

A

Misfolded proteins that causes disease

39
Q

Receptors and enzymes as drug targets

A

Most studied and largest groups of protein targets

40
Q

Carriers and transporters as drug targets

A

Have recognition sites for specific ligands

41
Q

Sttuctural proteins as drug targets

A

Most common in cancer, not usual target due to its low selectivity

42
Q

Peptide hormone as drugs

A

Insulin, Insulin lispro, and insulin aspart

43
Q

Insulin

A

Proline 28, glycine 29

44
Q

Insulin lispro

A

Proline 29, glycine 28

45
Q

Cutdown polypeptides as drugs

A

Part of the functional protein is given
Poor gut absorption
Rapid elimination
Trigger immuno response

46
Q

Monoclonal antibodies

A

Identical antibodies produced by identical b lympocyte

47
Q

Zumab

A

Humanized

48
Q

Umab

A

Human

49
Q

Momab

A

Mouse urine

50
Q

Ximab

A

Chimeric

51
Q

Immunoglobulins

A

Mixture of antibodies
Passive immunization

52
Q

Teriparatide (PTH)

A

Osteoporosis

53
Q

Etanercept

A

Rheumatoid arthritis

PHARM 113 (5 decks)

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