Biochem test 2

Question 1

Southern blots identify

Answer 1

DNA

Question 2

Western blots identify

Answer 2

protein

Question 3

northern blots identify

Answer 3

RNA

Question 4

what amino acids are hydrophobic

Answer 4

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

Question 5

Methionine

Answer 5

Met, M

Question 6

Phenylalanine

Answer 6

Phe, F

Question 7

pI (isoelectric point):

Answer 7

pH when a.a has no net charge

Question 8

Valine

Answer 8

V, Val

Question 9

Tryptophan

Answer 9

Trp, W

Question 10

linear tripeptide has

Answer 10

3 amino acids and 2 peptide bonds

Question 11

Peptide bond is also known as

Answer 11

amide bond

Question 12

Peptide bond formation is the reaction

Answer 12

NH2 and COOH from a.a.

Question 13

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

Answer 13

amino group

Question 14

What are the hydrophilic amino acids

Answer 14

Asparagine, Glutamine, Serine, Threonine

Question 15

What are the acidic amino acids

Answer 15

aspartic acid, glutamic acid

Question 16

What are the basic amino acids

Answer 16

Lysine, Histidine, arginine

Question 17

chaperonins such as the GroEl/Es system

Answer 17

requires ATP hydrolysis

Question 18

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

Answer 18

sickle cell anemia

Question 19

the formation of a dipeptide from two amino acids involves

Answer 19

loss of water

Question 20

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

Answer 20

1 primary structure can demtermine a 3 tertiary structure

Question 21

In general, molecular chaperone proteins function by

Answer 21

preventing premature folding by binding hydrophobic regions of the proteins

Question 22

What is true about peptide bonds

Answer 22

it results in linear polymer of amino acids

Question 23

How are peptide bonds synthesized

Answer 23

synthesized N-terminus to C-terminus

Question 24

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

Answer 24

2 amino acids

Question 25

Mass spectrometry has emerged as a technique for

Answer 25

protein sequencing.

Question 26

ELISA

Answer 26

enzyme linked immunosorbent assay

Question 27

What factors are used for protein sequencing

Answer 27

affinity, high salt concentration, ionic strength, size

Question 28

Membrane spanning contains

Answer 28

hydrophobic amino acids in the central region

Question 29

What does membrane spanning allow the protein to do

Answer 29

allow the protein to cross the bilayer membrane

Question 30

what are the two of Categorization of homologous sequences

Answer 30

Paralogs and orthologs

Question 31

Orthologs similar sequence is found in

Answer 31

different specicies

Question 32

Orthologs mode of evolution

Answer 32

conventional divergence -speciation

Question 33

Paralogs i Similar seq is found within the

Answer 33

the same species

Question 34

Paralogs Mode of evolution is

Answer 34

gene duplication

Question 35

What are some properities of hemoglobin

Answer 35

binds 4 O2 moderate affintiy to O2

Question 36

What is the elution order for ion exhange chromatography

Answer 36

weakly-charged → moderate → strongly-charge

Question 37

the column for ion Exhange chromatography is selected based on the

Answer 37

type and strength of charge

Question 38

affinity chromatography separates by

Answer 38

separates by molecular conformation

Question 39

affinity chromograhy frequntly generates

Answer 39

a single peak while all other in the sample is unretained

Question 40

.Bradford assay uses colorimetics to

Answer 40

measure the total amount of proteins.

Question 41

SDS-PAGE uses the charge to

Answer 41

separate proteins in different sizes.

Question 42

in gel filtration chromatography what particle elutes faster

Answer 42

Larger proteins elute first and smaller ones elute later.

Question 43

porus gels of gel filtration

Answer 43

separate small, denatured, or solubilized proteins

Question 44

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

Answer 44

x-ray crystallography

Question 45

Asparagine

Answer 45

Asn, N

Question 46

What is true about protein domains

Answer 46

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

Question 46

Carbon monoxide binds to heme-

Answer 46

with a higher affinity than oxygen

Question 47

Glutamine

Answer 47

Gln, Q

Question 48

Serine

Answer 48

Ser, S

Question 49

Threonine

Answer 49

Thr, T

Question 50

pI equivalence point

Answer 50

pI = (pK1 + pK2)/2

Question 51

pI for acidic a.a. (D, E

Answer 51

pI = (pK1 + pKR )/2

Question 52

Aspartic acid

Answer 52

Asp, d

Question 53

Glutamic acid

Answer 53

E,Glu

Question 54

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

Answer 54

(pK2 + pKR )/2

Question 55

What are the 10 essential amino acids

Answer 55

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

Question 56

Bovine insulin

Answer 56

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

Question 57

How much rotation is there on plane polorzed light

Answer 57

0

Question 58

What are some of the planer characteristics of a peptide bond

Answer 58

partial double bound character no rotation around the peptide bond

Question 59

α-carbon is

Answer 59

the point of flexibility along the backbone

Question 60

Φ and Ψ describe the

Answer 60

conformation of the backbone

Question 61

DNA binding fits perfectly to the

Answer 61

major groove of dsDNA

Question 62

What does DNA binding recognize?

Answer 62

* Recognize a specific DNA sequence and bind to it via H-bonds

Question 63

Whats a monomer

Answer 63

long a helix every 4th residue is hydrophobic

Question 64

What amino acids are in kertain

Answer 64

Large # of cys

Question 65

Why are their large # of cys in kertain

Answer 65

they stabilize the filament

Question 66

What does myoglobin do to O2

Answer 66

it stores O2

Question 67

Protein has minimal solubility at

Answer 67

pH=PI --- precipitation

Question 68

What are the 2 types of B sheets strucutres

Answer 68

parallel & antiparallel)

Question 69

What are the similarities between of parallel & antiparallel

Answer 69

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

Question 70

What are the differences between parallel and antiparallel

Answer 70

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

Question 71

what amino acids have ionizable side chains

Answer 71

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

Question 72

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

Answer 72

left hand fashion

Question 73

Sigmoidal O 2-binding curve:

Answer 73

very efficient in O 2 transport

Question 74

Heme causes the structural change, how

Answer 74

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