Lab Techniques Flashcards

(33 cards)

1
Q

What is the primary purpose of protein isolation?

A

To separate specific proteins from a complex mixture for analysis or use.

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2
Q

True or False: gas chromatography is a technique used to isolate proteins based on their specific interactions with ligands.

A

false

affinity chromatography

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3
Q

Fill in the blank: The technique used to separate proteins based on size is called __________.

A

gel electrophoresis

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4
Q

What is the role of SDS in SDS-PAGE?

A

To denature proteins and impart a negative charge for separation by size.

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5
Q

Which method uses a matrix to separate proteins based on their isoelectric point?

A

Isoelectric focusing

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6
Q

What does the term “purity” refer to in protein isolation?

A

The extent to which a protein is free from contaminants.

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7
Q

True or False: purification can be used to separate proteins based on their density.

A

false

centrifugation

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8
Q

What is the purpose of dialysis in protein purification?

A

To remove small molecules and salts from a protein solution.

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9
Q

What is the main principle behind size exclusion chromatography?

A

Separation based on the size of molecules, allowing smaller molecules to enter the pores of the matrix.

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10
Q

Which technique is commonly used to determine protein concentration?

A

Bradford assay

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11
Q

Fill in the blank: The __________ technique uses antibodies to specifically bind to proteins of interest.

A

immunoprecipitation

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12
Q

What does LC-MS stand for?

A

Liquid Chromatography-Mass Spectrometry

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13
Q

True or False: Western blotting is used to detect specific proteins after gel electrophoresis.

A

True

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14
Q

What is the significance of using a standard curve in protein assays?

A

To quantify unknown protein concentrations by comparison.

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15
Q

What type of chromatography separates proteins based on their charge?

A

Ion exchange chromatography

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16
Q

Fill in the blank: The __________ is a technique that separates proteins based on their thermal stability.

A

thermal shift assay

17
Q

What is the main advantage of using high-performance liquid chromatography (HPLC)?

A

Increased resolution and speed in separating proteins.

18
Q

True or False: The native PAGE technique preserves the protein’s native structure.

19
Q

What is the main purpose of a protein assay?

A

To measure the concentration of proteins in a sample.

20
Q

Which technique is best for analyzing protein-protein interactions?

A

Co-immunoprecipitation

21
Q

What is the role of a loading buffer in SDS-PAGE?

A

To provide density and color to the sample for loading into the gel.

22
Q

True or False: Mass spectrometry can provide information about the molecular weight of proteins.

23
Q

What does the term ‘fractionation’ refer to in protein isolation?

A

The process of separating proteins into different fractions based on specific properties.

24
Q

What is the key difference between analytical and preparative chromatography?

A

Analytical chromatography is used for analysis, while preparative chromatography is used for isolating large quantities of protein.

25
Fill in the blank: __________ is a technique that quantifies protein concentration by measuring absorbance at 280 nm.
UV-Vis spectroscopy
26
What is the significance of using a molecular weight marker in gel electrophoresis?
To estimate the size of unknown proteins in the gel.
27
True or False: Protein precipitation is a method to concentrate proteins from a solution.
True
28
What is the main use of a protein ladder in electrophoresis?
To determine the size of proteins by comparison.
29
What does the term 'denaturation' refer to in protein analysis?
The process of altering a protein's natural structure, typically through heat or chemicals.
30
Fill in the blank: The __________ assay measures the enzymatic activity of a protein.
enzyme activity
31
What does SDS in SDS-PAGE stand for?
Sodium Dodecyl Sulfate
32
Which technique would you use to analyze protein-protein interactions without denaturing the proteins?
Native PAGE
33
What is the main purpose of adding SDS to the protein sample in SDS-PAGE?
To impart a negative charge to the proteins and denature them