Test
Lab 3 | SDS PAGE
Este test tiene tipos de pregunta que se abren en el reproductor de siempre.
Preguntas del test (16)
1What is the function of 2-mercaptoethanol in a sample buffer prepared for SDS-PAGE?
- Areduce hydrophobic bonds
- Breduce disulfide bonds
- Cbreaks protein-protein interaction
- Dadds extra hydrogen atom
2The presence of glycerol in a sample buffer increases the density of protein sample that facilitates to prevent from diffusion in the sample well.
- AVerdadero
- BFalso
3Which tracking dye is used in SDS-PAGE?
- ASilver stain
- BBromothymol blue
- CBromophenol blue
- DCoomassie brilliant blue
4Which supporting matrix (gel material) is an ideal for separating protein in SDS-PAGE analysis?
- AAgarose
- BPolyacrylamide
- CAmmonium Persulfate (APS)
- DSodium Dodecyl Sulfate
5Which property of proteins best determines the electrophoretic pattern in SDS-PAGE under reducing conditions?
- Amolecular weight of subunits
- Bshape of the native protein
- Cspecific binding of the native protein
- Dnet charge of the native protein
6Which reagent (chemical) initiates polymerization in gel preparation for SDS - PAGE?
- ATetramethylethylenediamine (TEMED)
- BAmmonium Persulfate (APS)
- CBoth TEMED and APS
- D2-mercaptoethanol
7Which gel region has a lower percentage of acrylamide, allowing for higher porosity and faster migration of proteins?
- AResolving gel
- BStacking gel
8Which gel region is primarily responsible for separating proteins based on their molecular weight?
- ARunning gel
- BStacking gel
9Which gel region is located closer to the sample loading wells?
- ASeparating gel
- BStacking gel
10The [blank_start]long hydrophobic tail[blank_end] of the anionic detergent (SDS) disrupts the hydrophobic interactions of proteins, whereas the [blank_start]negatively charged sulfate group[blank_end] of SDS disrupts the ionic interactions.
- Along hydrophobic tail
- BNegatively charged sulfate group
- Cnegatively charged sulfate group
- D12 - Carbons
11Each band on the gel represents a different protein / protein subunit;
Smaller proteins move through the gel more [blank_start]rapidly[blank_end] than [blank_start]larger[blank_end] proteins and therefore are
found nearer the [blank_start]bottom[blank_end] of the gel.- Arapidly
- Bslowly
- Clarger
- Dsmaller
- Ebottom
- Ftop
12In order to accurately estimate protein molecular weight using PAGE, the proteins must be
- ANative
- BDenatured
13What is the effect of increasing the concentration of the gel in PAGE electrophoresis?
- AIt increases the migration speed of proteins
- BIt decreases the migration speed of proteins
- CIt has no effect on the migration speed of proteins
- DIt denatures the proteins
14Which the following statements is true about the stacking gel?
- ACompared to the running gel, the stacking gel has a basic pH (8.8)
- BIt is into this gel that the wells are formed and the proteins are loaded.
- CIt is on the bottom of the separating gel.
- DIt is used to quantify the protein sample before it enters the main separating gel.
15Which of the following methods is commonly used for separation of proteins by SDS PAGE?
- AAgarose - Vertical
- BAgarose - Horizontal
- CPolyacrylamide - Vertical
- DPolyacrylamide - Horizontal
16SDS used in denaturing PAGE is a 14-Carbon hydrophilic cationic detergent
- AVerdadero
- BFalso
Información
- Descripción
- Y1 Sem 2 BIC - Lab Test sobre Lab 3 | SDS PAGE, creado por Rand Haj Rubaeih el 04/04/2024.
- Autor
- Rand Haj Rubaeih
- Idioma
- English
- Visitas
- 24
- Etiquetas
- Valoración
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