Will our artificial enzyme,CelB-GFP, dissociate into subunits during SDS-PAGE? Why or why not?
Will our artificial enzyme,CelB-GFP, dissociate into subunits during SDS-PAGE? Why or why not?
Homework Answers
Yes it will dissociate. When the sds page takes place the it has denaturing nature and it denatures the protein into subunits and give them their native nature and enzymes are proteins so they also get denatured and dissociates into subunits
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Will our artificial enzyme,CelB-GFP, dissociate into subunits
during SDS-PAGE? Why or why not?
From an SDS-PAGE gel, how can you tell that you successfully induced GFP expression? Is that...
From an SDS-PAGE gel, how can you tell that you successfully induced GFP expression? Is that related to amount of bands?
Why is SDS-PAGE useful as an analytical tool, but not useful to purify your entire target...
Why is SDS-PAGE useful as an analytical tool, but not useful to purify your entire target enzyme?
Why do we use a ladder in SDS-PAGE gels? to determine SDS-PAGE electrical properties to determine...
Why do we use a ladder in SDS-PAGE gels? to determine SDS-PAGE electrical properties to determine protein size to determine nucleotide shape to determine protein shape
In the Western blot experiment, )Why are proteins treated with ionic detergent (SDS), reducing agents (DTT), and heat before SDS-PAGE Why do SDS-coated proteins migrate in an electric field? e...
In the Western blot experiment, )Why are proteins treated with ionic detergent (SDS), reducing agents (DTT), and heat before SDS-PAGE Why do SDS-coated proteins migrate in an electric field? e molecular mass of myosin light chain I is approximately 22 kD, myosin heavy chain is 200 kD ane actin is 42 kD, Which proteins will migrate fastest through the gel? Why?
In the Western blot experiment, )Why are proteins treated with ionic detergent (SDS), reducing agents (DTT), and heat before...
1-Define SDS-PAGE? 2-Explain why we use SDS (sodium dodecyl sulfate) in electrophoresis technique to separate proteins...
1-Define SDS-PAGE? 2-Explain why we use SDS (sodium dodecyl sulfate) in electrophoresis technique to separate proteins or nucleic acids? 3- Explain why TEMED should be the last reagent that add to the solution when preparing the gel?
Explain why isolated F1 subunits from the ATP synthase enzyme catalyze the hydrolysis of ATP. Use...
Explain why isolated F1 subunits from the ATP synthase enzyme catalyze the hydrolysis of ATP. Use protein structure, conformational changes, and free energy in your response.
You are investigating signaling pathways involved in the control of cell cycle. Why is SDS-PAGE well...
You are investigating signaling pathways involved in the control of cell cycle. Why is SDS-PAGE well suited in studies of cyclin modification but not in studies of retinoblastoma pRb phosphorylation?
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...
What are the two main types of enzyme inhibition occurring in our body, and why is...
What are the two main types of enzyme inhibition occurring in our body, and why is one occurring more frequently than the other?
please help Tor F. A) High molecular weight proteins will migrate farther during gel electrophoresis (SDS-PAGE)....
please help
Tor F. A) High molecular weight proteins will migrate farther during gel electrophoresis (SDS-PAGE). d) B-sheet protein structures can be stabilized by hydrogen bonding between distant residues on the same polypeptide. e) B-sheets are a type of secondary structure and are found in every protein.
Why do we use a ladder in SDS-PAGE gels? to determine SDS-PAGE electrical properties to determine protein size to determine nucleotide shape to determine protein shape
In the Western blot experiment, )Why are proteins treated with ionic detergent (SDS), reducing agents (DTT), and heat before SDS-PAGE Why do SDS-coated proteins migrate in an electric field? e molecular mass of myosin light chain I is approximately 22 kD, myosin heavy chain is 200 kD ane actin is 42 kD, Which proteins will migrate fastest through the gel? Why?
In the Western blot experiment, )Why are proteins treated with ionic detergent (SDS), reducing agents (DTT), and heat before...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...
please help
Tor F. A) High molecular weight proteins will migrate farther during gel electrophoresis (SDS-PAGE). d) B-sheet protein structures can be stabilized by hydrogen bonding between distant residues on the same polypeptide. e) B-sheets are a type of secondary structure and are found in every protein.
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