You have a mixture of positive, negative and neutral proteins. In order to obtain a pure positively charged protein, you can pass this mixture through a column containing G-50 coarse beads Anion Exchanger beads Cation Exchanger beads G-50 superfine beads
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You have a mixture of positive, negative and neutral proteins. In order to obtain a pure positively charged protein, you can pass this mixture through a column containing
G-50 coarse beads
Anion Exchanger beads
Cation Exchanger beads
G-50 superfine beads
Step by step
Solved in 2 steps
- A protein is allosterically regulated by a molecule. This molecule enhances the binding affinity, and is different from the normal ligand. How would you describe this molecule? A negative homotropic molecule A negative heterotropic molecule A positive heterotropic molecule A positive homotropic moleculeWhich of the following amino acids is most likely to be found in a beta sheet? a Nonpolar amino acids b Glycine c Polar charged amino acids d Polar uncharged amino acids e Proline"Loops of polypeptide that protrude from the surface of a protein often form the binding sites for other molecules" is true or false.
- Which of the following amino acid or types of amino acids are are rarely found in beta sheets? a. Polar charged amino acids b. Polar uncharged amino acids c. Non polar amino acids D. GlycineThe limit for G-200 beads is 5000-600,000. When you pass two proteins- Protein A (75, 000), Protein B (1,000,000), through these beads, the protein that will elute out last is – They both elute out at the same time. Protein B Protein AFor a protein that binds multiple ligands with negative cooperativity, which of the following is true? Each ligand bound increases the dissociation constant for subsequent ligands. Ligands cannot bind to the protein. The dissociation constant is not affected by binding of other ligands. Each ligand bound decreases the dissociation constant for subsequent ligands.
- Consider a protein in which a negatively charged glutamic acid side chain (pKa=4.2)(pKa=4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa=6.5)(pKa=6.5). Do only part B.Which one of the following is NOT a ligand?A. Glucagon B. Bacterial proteinC. AirUnder what pH conditions can a protein not bind to the beads in a column? pH = 7 pH = pI pH = pKa pH = -pKa
- Three proteins with an overall charges of 0, -5, and -8 are passed through an anion exchange column equilibrated in a buffer with low ionic strength and eluted with an increasing gradient of salt in a buffer. Which protein will elute last from the column? 1. Protein with no charge. 2. Protein with eight negative charges. 3. Protein with five negative charges. 4. Both charged proteins will elute at the same time.2,3 - BPG is ___________ charged, and is surrounded by __________ amino acids when it is bound to HB. a) Negatively; amino acids with positively charged side chains at pH 7 b) Negatively; amino acids with neutral charged side chains at pH 7 c) Negatively; amino acids with negatively charged side chains at pH 7 d) Positively; amino acids with positively charged side chains at pH 7Protein A will fold into its native state only when protein B is also present in the solution. However, protein B can fold itself into native confirmation without the presence of protein A. Which of the following is true? a. Protein B serves as precursor for protein A b. Protein B serves as molecular chaperone for protein A c. Protein B serves as ligand for protein A d. Protein B serves as structural motif for protein A
