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Biochem > Amino acids and Proteins > Flashcards

Amino acids and Proteins Flashcards

1
Q

Unbranched Nonpolar and Aliphatic aa’s

A

Gly, Ala, Pro

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2
Q

Branched Nonpolar and Aliphatic aa’s

A

Val, Leu, Ile

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3
Q

Nonpolar and Aliphatic aa’s

A

Gly, Ala, Pro, Val, Leu, Ile

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4
Q

Aromatic nonpolar aa’s

A

Phe

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5
Q

Aromatic more polar aa’s

A

Tyr, Trp

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6
Q

Aromatic aa’s

A

Phe, Tyr, Trp

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7
Q

Polar, uncharged aa’s

A

Asn, Gln, Ser, thr

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8
Q

Sulfur-containing aa’s

A

Met, Cys

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9
Q

Negatively (acidic) charged aa’s

A

Asp, Glu

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10
Q

Positively (basic) charge aa’s

A

Arg, Lys, His

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11
Q

Charged aa’s

A

Asp, Glu, Arg, Lys, His

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12
Q

3 aa’s with hydroxyl groups that thus act in kinases

A

Tyr, Ser, Thr

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13
Q

Only aa that is not chiral

A

Glycine

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14
Q

Orientation of nonpolar aa’s in proteins

A

to the inside

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15
Q

Orientation of uncharged/polar aa’s in proteins

A

To the outside

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16
Q

dimeric oxidized form of cysteine

A

Cystine

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17
Q

Name for dipolar ions

A

Zwitterions

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18
Q

7 Aa’s with ionizable side chains

A

Asp, Glu, His, Cys, Lys, Tyr, Arg

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19
Q

pH at which a molecule has a net charge of zero

A

Isoelectric point (pI)

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20
Q

condition in which there is reduced transport of cystine, causing stones

A

Cystinuria

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21
Q

Amino acid used in the synthesis of cysteine that can be given as treatment for kidney stones

A

Methionine

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22
Q

Agent that cleaves COOH- terminal of Met

A

Cyanogen bromide (CNBr)

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23
Q

Aa that is an alpha helix breaker

A

Proline

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24
Q

Secondary structure that is a right handed helix, with the carbonyl oxygen hydrogen bonded to the 4th amine hydrogen

A

Alpha helix

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25
Q

Amino acids required to create the reverse turn (beta turn) secondary structure of proteins

A

Proline and glycine

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26
Q

Supersecondary structure that mediates txn factor dimerization

A

Leucine zipper

27
Q

Supersecondary structure that is a DNA binding motif

A

Zinc finger

28
Q

Part of a polypeptide chain that can independently fold into a tertiary structure

A

Protein domain

29
Q

Example given of a protein domain

A

7 transmembrane receptor

30
Q

Fibrous protein composed of antiparallel beta pleated sheet
Strong, lacks elasticity

A

Fibroin (silk)

31
Q

Fibrous proteins composed of alpha helix that allows elasticity

A

Alpha keratin and tropomyosin

32
Q

Fibrous protein in wool, hair, and epidermal

A

Alpha keratin

33
Q

Fibrous protein that is a thin filament in muscle

A

Tropomyosin

34
Q

Fibrous protein formed when alpha keratin converts to a beta pleated sheet with heat or stretching

A

Beta keratin

35
Q

Components that maintain keratin secondary structure

A

Disulfides

36
Q

This secondary structure makes up beta keratins

A

beta pleated sheets

37
Q

Basic structural subunit of collagen

A

tropocollagen

38
Q

Structure of tropocollagen

A

Triple helix
Left-handend helix of ~1000aa (NOT an alpha helix)

39
Q

Aa required for tropocollagen helix formation

A

Glycine

40
Q

Condition caused by mutations in a1 or a2 chains of type I collagen

A

Osteogenesis imperfecta

41
Q

Condition which includes hyperextensible skin, hypermobile joints, bruising/bleeding tendencies

A

Ehlers-Danlos syndrome

42
Q

Enzyme that interconverts the cis and trans isomers of peptide bonds with proline

A

Cis-trans prolyl isomerase

43
Q

Enzyme that catalyzes disulfide bond formation and isomerization

A

Protein disulfide isomerase

44
Q

Autosomal recessive disease that involves a point mutation, changing a Glu to a Val

A

Sickle cell anemia

45
Q

Sickle cell anemia test where RBCs are deoxygenated with 2% sodium metabisulfite

A

Sickling test

46
Q

Sickle cell anemia test where hemolysates are deoxygenated with dithionite

A

Hb solubility test

47
Q

Disease that involves an accumulation of intraneuronal and extracellular bundles and filaments that form plaques

A

Alzheimer’s disease

48
Q

Disease in which the number of CAG’s in the associated gene is higher

A

Huntington’s disease

49
Q

Huntington’s disease has this abnormality in the HD gene

A

Higher number of CAG trinucleotide repeats; produces a string of Glutamine

50
Q

Centrifugation separates proteins by:

A

Size

51
Q

Milky or turbid appearance in centrifuged blood indicates what

A

lipids

52
Q

type of molecules that migrate faster in size exclusion chromatography

A

larger molecules (they bypass the beads)

53
Q

Type of charged proteins that are retained in Cation exchange (ion exchange chromatography)

A

Positively charged proteins (bind to negatively charged stationary beads)

54
Q

Type of charged proteins that are retained in Anion exchange (ion exchange chromatography)

A

Negatively charged proteins (bind to positively charged stationary beads)

55
Q

Protein analysis method that involves cell counting, sorting, and biomarker detection

A

Flow cytometry

56
Q

Protein analysis method that detects small amounts of protein or antibodies in cell extracts or body fluids

A

Enzyme-linked immunosorbent assay (ELISA)

57
Q

type of ELISA that can test blood for specific infection

A

Indirect ELISA

58
Q

Type of ELISA that involves Ag coated well and when a specific Ab binds, an enzyme linked Ab will bind to that specific Ab

A

Indirect ELISA

59
Q

Type of ELISA that involves a monoclonal Ab coated well, causing Ag to bind to the Ab, and a second monoclonal Ab linked to an enzyme binds the immobilize Ag

A

Sandwich ELISA

60
Q

Proteins that move faster in SDS-PAGE

A

Smaller (lower molecular weight) proteins

61
Q

SDS-PAGE separates proteins by:

A

Size (NOT charge)

62
Q

Protein analysis method that may be used to quantitate the amount of a specific protein in a sample

A

Western blot

63
Q

Protein analysis method where proteins can be separated based on their relative content of acidic and basic amino acid residues

A

Isoelectric focusing (IEF)

Biochem (21 decks)

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