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*Short Response*
Electrophoresis is defined as the migration of charged particles under the influence of electric field. An electrophoretic system consists of two electrodes of opposite charge (anode, cathode), connected by a conducting medium called an electrolyte. Factors affecting electrophoresis are-
1. Size of ion/ molecule
2. Charge of ion/ molecule
3. Temperature
4. Ionic strength of the buffer
5. Potential difference/voltage applied
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- 4,5,6 please answer all give the significance/role/effect of the reagent/condition in the isolation or analysis of a biomolecule. limit answers to two short sentencesQuestion 9. Which of thefollowing is not formed through adehydration synthesis reaction?A. polysaccharideB. polypeptideC. Nucleic acidD. phospholipidE. glycerolPaper Chromatography question 1. If there are two unknown samples yielded the same Rf value in the paper chromatography result, can we directly conclude that those two samples are identical? Explain briefly
- Text:QUESTION 16 Protein maturation in the ER includes. A Disulfide bond formation B. proteolytic cleavage C attachment of oligosaccharide d. Prolyl isomertzationColumn Chromatography Question 1. We were tasked to use a microcolumn in a certain experiment. why do we need to be careful and be catious when we place the sample inside the microcolumn. 2. Why is it important that the level of elution of the solvent go below the top of the adsorbent?Experiment No. 2 AMINO ACIDS AND PROTEINS Data Solubility in water Sample Solubility (Soluble, Partially Soluble, Insoluble) Color with red litmus paper Color with blue litmus paper Is the solution acidic, basic, or neutral? alanine glutamic acid arginine albumin Color Reactions of Amino Acids Ninhydrin Test Color of Ninhydrin solution: ___________________________________ Sample Color original solution Color with Ninhydrin Color after 10 min. alanine glycine glutamic acid tyrosine albumin Biuret Test Color of 3% CuSO4 solution: _____________________________________ Sample Color of original solution Color after NaOH/CuSO4 casein alanine albumin gelatin distilled water Molisch Test Color of…
- *Answer only question 2. Prelude is in Question 1. 1. Briefly explain the principle behind the following techniques:(a) ion-exchange chromatography (b) gel filtration chromatography (c) affinity chromatography 2. Use three diagrams to illustrate the separation of three different proteins by these methods.Question for protein crystallography- 1. While performing a routine protein crystallization screening, you observe that one of your well drops has doubled in size compared to the remaining wells. Note: the drop in question was set up by taking 1 µL of the protein solution (10 mg/mL LDH in 20 mM TRIS pH 7.5, 0.5 M NaCl and 10% PEG 4000K) and adding it to 1 µL of the crystallization solution (10% PEG 4000K, 50 mM NaCl and 20 mM TRIS pH 8.0). Why did this drop grow larger in size compared to when you initially set it up?question: What is the purpose of adding table salt into the solution? What reagent is used in research labs/ Is it also table salt (NaCl)?
- Question based on SDS-PAGE You are working with a 60 kDa protein that you want to visualize on a SDS-PAGE. What % separating gel will you use in your SDS-PAGE?Result and Discussion: Pauly Reaction: Samples: tyrosine, alanine, histidine Reagents: Cold Saturated Sulfanilic Acid, Cold 1 % Sodium Nitrite (NaNO2) and 10% Sodium Bicarbonate (Na2CO3) - Mix 0.5 ml of cold saturated sulfanilic acid solution (HANDLE WITH CARE) with 0.25 ml of cold 1.0% NaNO2. Cool in ice with constant shaking for 3 minutes. Add 0.5 ml of the sample and make alkaline with 10% Na2CO3. Record your observation.The structural elucidation of cellular proteins will help to better understand cell physiology. This can be achieved by a. Subcellular fractionation & ion exchange chromatography b. Polyacrylamide gel electrophoresis & nuclear magnetic resonance c. Ion exchange chromatography & polyacrylamide gel electrophoresis d. Nuclear magnetic resonance & X-ray crystallography