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Biochem midterm exam 1 > Biochem test 2 > Flashcards

Biochem test 2 Flashcards

1
Q

Southern blots identify

A

DNA

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2
Q

Western blots identify

A

protein

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3
Q

northern blots identify

A

RNA

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4
Q

what amino acids are hydrophobic

A

alanine, valine, leucine,
Isoleucine
Methionine, Phenylalanine,
Tryptophan
Tyrosine

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5
Q

Methionine

A

Met, M

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6
Q

Phenylalanine

A

Phe, F

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7
Q

pI (isoelectric point):

A

pH when a.a has no net charge

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8
Q

Valine

A

V, Val

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9
Q

Tryptophan

A

Trp, W

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10
Q

linear tripeptide has

A

3 amino acids and 2 peptide bonds

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11
Q

Peptide bond is also known as

A

amide bond

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12
Q

Peptide bond formation is the reaction

A

NH2 and COOH from a.a.

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13
Q

In the side chane of Lys what group is attached to the c group

A

amino group

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14
Q

What are the hydrophilic amino acids

A

Asparagine, Glutamine, Serine, Threonine

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15
Q

What are the acidic amino acids

A

aspartic acid, glutamic acid

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16
Q

What are the basic amino acids

A

Lysine, Histidine, arginine

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17
Q

chaperonins such as the GroEl/Es system

A

requires ATP hydrolysis

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18
Q

What is the name of disease caused by a missense mutation in the B chain of hemoglobin

A

sickle cell anemia

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19
Q

the formation of a dipeptide from two amino acids involves

A

loss of water

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20
Q

the classic experiment demonstrating that reduced and denatured RNase A could refold into the native form demonstrates that

A

1 primary structure can demtermine a 3 tertiary structure

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21
Q

In general, molecular chaperone proteins function by

A

preventing premature folding by binding hydrophobic regions of the proteins

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22
Q

What is true about peptide bonds

A

it results in linear polymer of amino acids

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23
Q

How are peptide bonds synthesized

A

synthesized N-terminus to C-terminus

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24
Q

peptide bond formation is achieved by the dehydration condensation of how many amino acids

A

2 amino acids

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25
Q

Mass spectrometry has emerged as a technique for

A

protein sequencing.

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26
Q

ELISA

A

enzyme linked immunosorbent assay

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27
Q

What factors are used for protein sequencing

A

affinity, high salt concentration, ionic strength, size

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28
Q

Membrane spanning contains

A

hydrophobic amino acids in the central region

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29
Q

What does membrane spanning allow the protein to do

A

allow the protein to cross the bilayer membrane

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30
Q

what are the two of Categorization of homologous sequences

A

Paralogs and orthologs

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31
Q

Orthologs similar sequence is found in

A

different specicies

32
Q

Orthologs mode of evolution

A

conventional divergence -speciation

33
Q

Paralogs i Similar seq is found within the

A

the same species

34
Q

Paralogs Mode of evolution is

A

gene duplication

35
Q

What are some properities of hemoglobin

A

binds 4 O2
moderate affintiy to O2

36
Q

What is the elution order for ion exhange chromatography

A

weakly-charged → moderate → strongly-charge

37
Q

the column for ion Exhange chromatography is selected based on the

A

type and strength of charge

38
Q

affinity chromatography separates by

A

separates by molecular conformation

39
Q

affinity chromograhy frequntly generates

A

a single peak while all other in the sample is unretained

40
Q

.Bradford assay uses colorimetics to

A

measure the total amount of proteins.

41
Q

SDS-PAGE uses the charge to

A

separate proteins in different sizes.

42
Q

in gel filtration chromatography what particle elutes faster

A

Larger proteins elute first and smaller ones elute later.

43
Q

porus gels of gel filtration

A

separate small, denatured, or solubilized proteins

44
Q

a technique used to determine the tertiary structure of a protein is -

A

x-ray crystallography

45
Q

Asparagine

46
Q

What is true about protein domains

A

they may retain their correct shape even when seperated from the rest of the proteins

46
Q

Carbon monoxide binds to heme-

A

with a higher affinity than oxygen

47
Q

Glutamine

48
Q

Serine

49
Q

Threonine

50
Q

pI equivalence point

A

pI = (pK1 + pK2)/2

51
Q

pI for acidic a.a. (D, E

A

pI = (pK1 + pKR )/2

52
Q

Aspartic acid

53
Q

Glutamic acid

54
Q

pI for basic a.a. (K, R, H)

A

(pK2 + pKR )/2

55
Q

What are the 10 essential amino acids

A

Phenylalanine (F)
Lysine (K)
Leucine (L)
Tryptophan (w)
Arginine (R)
Methionine (M)
Valine (V)
Histidine (H)
Threonine (T)
Isoleucine (I)

56
Q

Bovine insulin

A

two polypeptide chains A and B joined by disulfide (S–S) bonds

57
Q

How much rotation is there on plane polorzed light

58
Q

What are some of the planer characteristics of a peptide bond

A

partial double bound character
no rotation around the peptide bond

59
Q

α-carbon is

A

the point of flexibility along the backbone

60
Q

Φ and Ψ describe the

A

conformation of the backbone

61
Q

DNA binding fits perfectly to the

A

major groove of dsDNA

62
Q

What does DNA binding recognize?

A
  • Recognize a specific DNA sequence and bind to it via H-bonds
63
Q

Whats a monomer

A

long a helix
every 4th residue is hydrophobic

64
Q

What amino acids are in kertain

A

Large # of cys

65
Q

Why are their large # of cys in kertain

A

they stabilize the filament

66
Q

What does myoglobin do to O2

A

it stores O2

67
Q

Protein has minimal solubility at

A

pH=PI — precipitation

68
Q

What are the 2 types of B sheets strucutres

A

parallel & antiparallel)

69
Q

What are the similarities between of parallel & antiparallel

A

Inter-strand H-bonding between C=O & N-H

70
Q

What are the differences between parallel and antiparallel

A

the direction of the associated β strands and the length of loop

71
Q

what amino acids have ionizable side chains

A

arginine, aspartic acid, cysteine, glutamic acid, histidine, lysine and tyrosine

72
Q

In Keratin, pairs of helices wind about each other in what fashion

A

left hand fashion

73
Q

Sigmoidal O 2-binding curve:

A

very efficient in O 2 transport

74
Q

Heme causes the structural change, how

A

Binding of O 2 → Fe(III) into heme plane → Pull on helix F → Conformational
change

Biochem midterm exam 1 (10 decks)

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