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MBD > FINALS - Protein Analysis > Flashcards

FINALS - Protein Analysis Flashcards

1
Q

what is the most abundant macromolecules in the biological system

A

proteins

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2
Q

proteins are polymers comprising amino acid that are linked by ______

A

peptide bonds

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3
Q

True or False:

proteins serve as:
1. antibodies
2. enzymes
3. messengers
4. structural components
5. transport
6. transport or storage molecule

A

true

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3
Q

the proteins that can be detected in the blood of the patient are called?

A

biomarkers

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4
Q

these are measurable substance in the blood whose presence is indicative of diseases or environmental exposure

A

biomarkers

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5
Q

most common method for purifying proteins from other protein molecules with a given sample

A

column chromatography

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6
Q

this involves the separation of soluble components in a solution by specific differences in PHYSICAL-CHEMICAL CHARACTERISTICS of the different constituents

A

column chromatography

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7
Q

what does the column chromatography uses to separate proteins based on their physical properties?

A

glass or plastic tube with resin inside

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8
Q

what should be added in the column for proteins to migrate?

A

buffer solution

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9
Q

the proteins the sample of a column migrate depending on?

A
  1. nature of the matrix
  2. physical properties
  3. chemical properties
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10
Q

in this protein analysis technique, the resin bead has many tiny pores like a WHIFFLE BALL

A

gel permeation/filtration/size exclusion

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11
Q

in gel permeation, the molecules are separated based on their difference in?

A

size and shape

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12
Q

in gel permeation, small molecules are more likely to go through the?

A

pore of the matrix

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13
Q

true or false:

in gel filtration, large molecules move through the column more slowly since they cannot fit into the beads

A

false; quickly

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14
Q

separates proteins using resin according to their SURFACE CHARGES

A

ion exchange chromatography

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15
Q

it uses the LOCK AND KEY BINDING that is widely present in biological system

A

affinity chromatography

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16
Q

it is used to separate and prepare LARGER quantities of PROTEINS and ANTIBODIES

A

affinity chromatography

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17
Q

it uses the principle that the protein binds to molecules for which it has SPECIFIC AFFINITY

A

affinity chromatography

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17
Q

this is the specific affinity where the PROTEIN BINDS TO CARRY OUT BIOLOGICAL ACTIVITY

A

ligand

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18
Q

its purpose are for SEPARATION, to determine SIZES, PRESENCE/AMOUNT OF DNA

A

electrophoresis

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19
Q

in electrophoresis, what is used to carry out proteins with a STACKING GEL and SEPARATING GEL?

A

polyacrylamide gel electrophoresis (PAGE) with SDS

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20
Q

this technique is associated with STAINING METHOD and can DETECT BAND OF PROTEIN in a simple and relatively rapid manner

A

electrophoresis

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21
Q

this DISRUPTS the structure of protein to be LINEAR and bind most protein

A

sodium dodecyl sulphate (SDS)

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22
Q

give the agents that is used in SDS for denaturation and breaking of covalent bonds

A

dithiothreitol (DTT) or 2-mercaptoethanol

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23
Q

this is often used to determine the MOLECULAR WEIGHT of proteins

A

SDS

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24
Q

each sodium dodecyl sulfate contributes to how many negative charges?

A

two

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25
Q

can detect as low as 10 ng - 1 ng of protein bands

A

colorimetric

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26
Q

organic dye and most frequently employed method for protein detection in SDS-PAGE gel

A

coomassie blue staining

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27
Q

uses IMIDAZOLE AND ZINC SALTS for protein detection in electrophoresis gels

A

zinc-reverse staining/negative staining

28
Q

based on the BINDING OF SILVER IONS to the proteins followed by reduction to free silver, sensitization, and enhancement

A

silver staining

29
Q

spots in silver staining are _____ on a ____ background

A

dark brown to black; light beige

30
Q

what is used to solve differentially sensitive proteins to silver staining?

A

glutaraldehyde free modified silver staining

31
Q

it bands FLUORESCE

A

fluorescence

31
Q

better resolving power as compared to the SDS-PAGE

A

two-dimensional gel electrophoresis

32
Q

the most popular and well-established technique for GLOBAL PROTEIN SEPARATION AND QUANTIFICATION

A

gel-based proteomics

33
Q

this is an example of a gel-based proteomics

A

two-dimensional gel electrophoresis

34
Q

protein in 2DE is electrophoresed through a narrow tube gel containining molecules called?

A

ampholytes

35
Q

ampholytes set up a _____

A

pH gradient

36
Q

this is the pH at which protein has no net charge/neutral

A

isoelectric point

37
Q

results after isoelectric focusing and SDS-PAGE are visualized and quantified through?

A

bioinformatic software

38
Q

northern blot is for?

A

RNA

39
Q

southern blot is for?

A

DNA

40
Q

western blot is for?

A

proteins

41
Q

this is a laboratory method used to detect SPECIFIC PROTEIN molecules among a MIXTURE of proteins

A

western blot

42
Q

what solid support is used in western blotting in transferring the gel

A

nitrocellulose/nylonsheet/or PVDF (polyvinyl vinylidene difluoride)

43
Q

this mode of transferring proteins is aided by capillary action or vacuum

A

diffusion/passive transfer

44
Q

achieved by posing a membrane sheet on one or both side of the gel

A

diffusion/passive transfer

45
Q

mode of transferring proteins by putting a gel membrane in a suitable holder and immersing both the gel and membrane in a tak filled with buffer fitted with TWO PLATE ELECTRODE (- and +)

A

electroblotting/electrotransfer

46
Q

these binds to the non-specific protein binding sites to prevent the binding of the antibodies to these sites

A

blocking agents

47
Q

these generates a colored product that could be conjugated to an enzyme

A

horseradish peroxidase (HRP) and alkaline phosphatase

48
Q

almost same with the color formation wherein it provides HIGHER SENSITIVITY than the COLOR PRODUCTION system

A

chemiluminescent

49
Q

in UV absorption method, what can be used in detecting proteins?

A

spectrophotometer

50
Q

the principle of this method is that nucleic acids (DNA or RNA) contain conjugated double bonds in their purine and pyrimidine rings that have a specific ABSORPTION PEAK at 260 nm

A

UV absorption peak

51
Q

the most commonly used reference protein in colorimetric

A

bovine serum albumine (BSA)

52
Q

in this method the peptide bonds of protein react with CUPRIC IONS present in BIURET reagents under alkaline condition

A

biuret method

53
Q

if cupric ions reacvct with biuret reagents it will produce a _____ color

A

purple

54
Q

presence of protein in biuret method will produce what color

A

violet

55
Q

this is based on the BIURET REACTION with ADDITIONAL steps and reagents to increase the sensitivity of detection

A

lowry protein assay

56
Q

in the biuret reaction, copper interacts with four nitrogen atoms of peptides that forms ____

A

cuprous complex

57
Q

reacts with cupric ions generated by the BIURET REACTION under ALKALINE condition forming BCA CUPROUS COMPLEX forming a purple color

A

bicinchonic acid method

58
Q

this is a common laboratory technique which is used to MEASURE THE CONCENTRATION of an ANALYTE in a solution

A

ELISA

59
Q

ability to DISCRIMINATE among DIVERSE protein

A

specificity

60
Q

ability to TIGHTLY BIND to molecules

A

afiinity

61
Q

what produces the chemical interaction between antibodies in ELISA

A

B cells of leukocytes and antigens

62
Q

y-shaped; any foreign substances

A

antigen

63
Q

green color attached to antigen

A

antibody

64
Q

uses a primary labeled antibody that react DIRETCLY with the antigen

A

direct ELISA

65
Q

it only uses an enzyme-labelled PRIMARY antibody; SECONDARY antibodies are not needed

A

direct ELISA

66
Q

it utilizes a primary UNLABELED antibody in conjunction with a labeled SECONDARY antibody

A

indirect ELISA

67
Q

antigens like TUMOR MARKERS, HORMONES, SERUM PROTEINS may be determined and bind with the capture antubody and become IMMOBILIZED

A

sandwich ELISA

68
Q

uses to determine the PRECISE MASS of PEPTIDES

A

MALDI-TOF spectrometry

69
Q

The peptides are immobilized in an organic MATRIX and then blasted with a LASER, causing them to be ejected in the form of an ionized gas.

A

MALDI-TOF

MBD (5 decks)

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