What effect will phosphorylation have on the behaviour of a protein on a 2Dgel?1. The spot corresponding to phosphorylated protein will be in the sameposition as that of unphosphorylated one.2. Phosphorylated protein will run slower in the second dimension (SDSPAGE).3. Compared to the spot of unphosphorylated protein, the spotcorresponding to phosphorylated protein will focus during separation in thefirst dimension in an area with lower pH.4. There will be shifts during both separation stages.O 3O 1O 4O 2

Phosphorylation is the post translation modification of proteins. Phosphorylation generally occurs…

Answered: What effect will phosphorylation have…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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You are studying the rate of actin polymerization and depolymerization in an in-vitro hypothetical system. The G actin concentration in the solution of the experimental setup is 0.3μm. Based on the data values predict the outcome of the experiment. Please note that X or Y ends can be "any end" of the actin filament. -1 X end actin: Association rate: 10 µmS-¹ ; Dissociation rate: 2.5 µmS-¹ Y end actin: Association rate: 5 µmS-¹ ; Dissociation rate: 2.5 µmS-¹ O The X end of the actin filament will grow. O Neither X or Y end of the filament will grow. O The Y end of the actin filament will grow. O There is not sufficient data to predict the
14. A protein mixture consisting of proteins A, B, and C was subjected to various protein purification steps. First, the protein mixture was applied to an anion ion exchange column. When the column was washed with an increasing concentration gradient of chloride ions, the order of elution of the three proteins was B, then C, and finally A. Next, the protein mixture was chromatographed on a gel filtration column. The order of elution of the three proteins from this column was C, A, B. Finally, the protein mixture was passed over a chromatography column containing a Ni-NTA affinity matrix. Only protein A was retained by the column. Answer the following (i) Which protein (A, B, or C) has the highest and lowest positive charge (ii) Which protein has the highest and lowest mass (ii) Which protein has an affinity for the Ni-NTA matrix and why
How will the temperature affect the sequence of proteins when ribosome stalling is done in vivo? 2 possible results? how might the temperature affect the sequence of proteins? is there less ribosome stalling at all sites or some locations specifically and why? where is the stalling happening specifically? is there less stalling at all sites or some locations? why might that be? how can raisning the tempreture affect the hydrogen bonds in the ribosome? how can raising the tempreture affect the hydrogen bonds in the ribosome?
Same question but two different sections
Imagine you need to move a large protein from one region in the cell to another. Which of the following proteins would be able to do this? Onuclease O myoglobin O kinesin Oligase O hemoglobin O myosin
9. Shown below is a binding pocket for a protein with a ligand bound. The ligand interacts with a serine and a valine side chain. ligand a. Briefly explain, in terms of Ka, the effect of a mutation that replaces the serine residue with a valine residue. b. Briefly explain, in terms of Kd, the effect of a mutation that alters the ligand (as seen below) binding to the original, unmutated, binding site. :0: ligand 2
Why does in this experiment, after gel is formed from gelatin the marble in papaya juice to the first cup (Lot A), second cup (Lot B) and 10 ml of kiwi juice to the third cup (Lot C) disappeared? While in fourth cup (control) the marble did not disappear it just float on the surface. What is the action of protease on gelatin?
7. Specificity of membrane transporters. A protein that transports amino acids across the cell membrane was found to bind only a few amino acids efficiently. To find the specificity, many different amino acids and substrate analogs were used as competitive inhibitors in transport studies at pH 5.9 with L-histidine (Km = 10 μM). The Ki values calculated from Lineweaver-Burk plots are shown in the table below. Comparing the structures of L-histidine and the competitive inhibitors (for which most of them, you should know their structures!), what can you conclude about the characteristics of molecules that this transport protein binds at its active site? K; (10-€ M) Amino acid or analog L-Lys L-Arg Gly L-Asp D-His Histamine Dehydrourocanate D-Arg 2 3 285 450 340 390 285 355 HN- + HN + Structure -ΝΗ -NH3 histamine ΝΗ -COO™ dehydrourocanate
4. Deducing quaternary structure via SDS-PAGE. SDS-PAGE is a convenient method for separating polypeptides solely on the basis of size. Small polypeptides travel faster than large ones; rate of migration through the gel is inversely proportional to the logarithm of molecular weight. The subunit structure of a multimeric protein often can be deduced using this technique in conjunction with a protein cross-linking agent. Cross-linking agents react with amino acid residues of two polypeptides that are in contact, thereby linking them by covalent bonds. After limited treatment with the reagent, so that some but not all subunits become cross-linked to their neighbors, the protein is subjected to SDS-PAGE and the molecular weights of the resulting proteins (bands) are estimated. The results of such experiments on two proteins (Protein A and Protein B) are shown below. What is the most likely subunit structure of each protein? Protein A SDS-PAGE cross-linking agent MW 105,000 70,000 35,000…
1. The CFTR protein is a chloride channel in the cell membrane. Use your understanding of the biochemical properties/categories of amino acids and how they interact with membrane phospholipids to predict the distribution of charged/polar, and non-polar amino acids within the domains of CFTR listed below. Consider one category to include the charged amino acids and the polar amino acids and the other category to include the non-polar amino acids. For each domain, predict which category of amino acids is likely to be most abundant. Also, explain the rationale behind your prediction. Protein domain Prediction (Charged/Polar or Non-Polar amino acids?) Explanation for prediction TMD1 and TMD2 (transmembrane domains, parts 1-12) ECLs and ICLs (extracellular and intracellular loops) NBD1 and NBD2 R
The role of GTP hydrolysis in actin polymerization is similar to the role of ATP hydrolysis in tubulin polymerization: both serve to weaken the bonds in the polymer and thereby promote depolymerization. Is that true or false? why?
What specific molecule gives rise to the stability and fluidity of the membrane and what are the biochemical properties of this molecule that cause fluidity and stability? A- B I F @ 2 7

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