Gel Electrophoresis Electrophoresis of histones and myoglobin under non-denaturing conditions (pH = 7.0) results in both proteins migrate to the cathode histones migrate to the cathode and myoglobin migrates to the anode histones migrate to the anode and myoglobin migrates to the cathode both proteins migrate to the anode both proteins migrate to the cathode histones migrate to the cathode and myoglobin migrates to the anode histones migrate to the anode and myoglobin migrates to the cathode both proteins migrate to the anode ANSWER DOWNLOAD EXAMIANS APP
Gel Electrophoresis In isoelectric focusing, proteins are separated on the basis of their relative content of positively charged residue only relative content of negatively charged residue only relative content of positively and negatively charged residue size relative content of positively charged residue only relative content of negatively charged residue only relative content of positively and negatively charged residue size ANSWER DOWNLOAD EXAMIANS APP
Gel Electrophoresis Proteins are separated in an SDS-PAGE experiment on the basis of their negatively charged side chains molecular weight positively charged side chains different isoelectric points negatively charged side chains molecular weight positively charged side chains different isoelectric points ANSWER DOWNLOAD EXAMIANS APP
Gel Electrophoresis In an SDS-PAGE proteins are denatured by the SDS smaller proteins migrate more rapidly through the gel proteins have the same charge-to-mass ratio All of these proteins are denatured by the SDS smaller proteins migrate more rapidly through the gel proteins have the same charge-to-mass ratio All of these ANSWER DOWNLOAD EXAMIANS APP
Gel Electrophoresis The subunit molecular weight as well as the number of subunits in the quaternary structure can be determined by combining information from (a)and (b) SDS-PAGE electrophoresis isoelectric focusing gel filtration chromatography combining information from (a)and (b) SDS-PAGE electrophoresis isoelectric focusing gel filtration chromatography ANSWER DOWNLOAD EXAMIANS APP
Gel Electrophoresis In SDS-PAGE, the protein sample is first treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis treated with a oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis None of these fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent. treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis treated with a oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis None of these fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent. ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS