Macromolecules_Result_Record (1)

Two dimensional electrophoresis separates proteins according to their isoelectric focusing and mass. True False

Topic: Determination of Protein Concentration by Spectrophotometry: The Standard Curve   The use of Beer-Lambert’s law to estimate the concentration of protein samples is limited only to dilute solutions. Explain why

The reults for the macroscopic part: 0.30M glycerin – solution was translucent (could see text behind the test tube) 0.15M NaCl – solution was opaque (could not see text behind the test tube) 0.30M NaCl – solution was opaque (could not see text behind the test tube) 0.15M glucose – solution was translucent (could see text behind the test tube) 0.30M glucose – solution was opaque (could not see text behind the test tube) 0.30M Urea – solution was translucent (could see text behind the test tube) Results for microscopic part: 0.30M glycerin – no cells present 0.15M NaCl – normal sized cells 0.30M NaCl – crenated (shrunken and star-shaped) cells 0.15M glucose – no cells present 0.30M glucose – normal sized cells 0.30M Urea – no cells present Determine the osmolarity (hypoosmotic, isosmotic, or hyperosmotic) and tonicity (hypotonic, isotonic, hypertonic) of the following solutions.In which solutions did the osmolarity NOT match the tonicity? For those solutions, why did the osmolarity…

Multiple choice   Which compound will yield a positive result with Salkowski test? (Picture 1) A, B, C, D In the emulsification of fats, which species is water soluble? (Picture 2) A, B, C, D In the emulsification of fats, which species is hydrophobic? (Picture 2) A, B, C, D

Ninhydrin Test Reagent’s Composition   Observations:   Inferences: What is the principle behind this test?     Can ninhydrin test distinguish amino acids and proteins? Can this test be used to detect the presence of proteins in a sample? Elaborate your answers.

COLOR REACTIONS OF PROTEINS AND AMINO ACIDS answer this please asap

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…

Total Protein Determination Spectroscopy Values CREATE CALIBRATION CURVE? DRAWN CONCENTRATION AND ABSORPTION CURVE

The concentration of protein in a solution can be determined via UV spectroscopy and colorimetry* techniques. Explain further on the statement, give examples of the techniques (please provide three examples for the colorimetry), general principles/mechanism, and general procedures of the techniques. You may use a Table to present the answer. If you need to choose a technique to measure your protein sample, what would be your choice? Justify your answer.

Answer the following questions about protein concentration determination. a) At what wavelength should an albumin protein solution placed in a quartz cuvette be measured in the spectrophotometer? Why is that? b) With which methods other than spectrophotometer can the amount of protein be measured quantitatively?

Using my chart can you help me with this question. The tests we used were qualitative; they allowed us to determine if a biological molecule was present or absent. In contrast, what type of information would a quantitative test provide?

Report Sheet: Proteins (page 3) What kind of protein is casein? Name: POST-LABORATORY QUESTIONS: What is the isoelectric point of casein? What is acid in our sour milk? How is it produced? What type of chemical grouping is present in all proteins? How many of these chemical groupings must be present in a molecule to give a positive Biuret test? Give the principle involved and the chemical structure responsible for the positive Biuret Test? Can you distinguish proteins and other amino compounds by the Ninhydrin test? Explain. 30 | Biochemistry

In protein electrophoresis, what reagent present  in the sample buffer is used to eliminate differences in the charge densities of proteins?   Tris-HCL ph 8.8   2-mecraptothanol   SDS(sodium dodecyl sulfate)   Tris-HCL PH 6.8

An unknown sample was tested if there is a presence of lipid, after the test it shows that it is positive for translucent test, soluble with chloroform, produced a pungent odor in acrolein test, produced a red color for Baudouin Test, and the violet color disappeared in Huble’s Test. What is the sample? Group of answer choices A lipid that is saturated, contain glycerol, and sesame oil A lipid that is saturated, doesn’t contain glycerol, and sesame oil A lipid that is unsaturated, doesn’t contain glycerol, and sesame oil A lipid that is unsaturated, contain glycerol, and sesame oil

Table 4- Determination of the optimum pH of catechol oxidase enzyme Potato extract (mL) Tube # 2d 3d 4d 5d 6d 7d dH₂O (mL) 0 0 0 0 0 0 Catechol (mL) 6 6 6 6 6 6 pH buffer added 4mL pH 2 4mL pH 4 4mL pH 6 4mL pH 7 4mL pH 8 4mL pH 10 1 1 1 1 1 1 Absorbance (0 mins) A: 0.010 Start Time: 3:24 A: 0.008 Start Time: 3:34 A: 0.023 Start Time: 3:36 A: -0.006 Start Time: 3:36 0.018 A: Start Time: 3:36 A: 0.011 Start Time: 3:36 Absorbance (after 10 mins in 40°C water bath) -0.030 A: Take reading at: 3:44 A: 0.154 Take reading at: 3:46 A: 0-105 Take reading at: 3:46 A: 0-132 Take reading at: 3:46 A: 0.074 Take reading at: 3:46 A: 0.018 Take reading at: 3!46 Q15) What is the enzyme's optimum pH(s)? Answer: Q16) Use the difference between 2nd and 1st absorbance to support your conclusion for the optimum pH. Subtract Omin from 10min absorbance -0.04 0.0012 0.082 0.138 0.056 0.007

There are two proteins in a pH 7 buffer, what you know is: one has a lot of Asp and Glu, the other one has a lot of Lys, Arg and His. Below which approach will get the two proteins separated? gel filtration chromatography ultracentrifugation salting out ion exchange chromatography affinity chromatography

Consider a mixture comprised of the proteins below: Protein that will most strongly bind to an anion exchange column is? Protein that will elute first in gel filtration chromatography is? Protein that will elute last in hydrophobic interaction chromatography is? Protein that will elute last in carbohydrate containing column is ?

Purpose: what is the concentration of the menown Solution? Hypothesis: None. Method: Use the transport Activity - dry run to get the method Independent Variable Dependent Variable (measuring) (changing) Different molarinies of sucrose Procedure: "as given" Data Table: Molarity in bag 0 (H₂0) 0.2 M Sucrose 0.4 M Sucrose 0.6 M Sucrose 0.8 M Sucrose 1.0 M Sucrose Unknown 90 38 40 initial mass (g) 20 10 10 10 10 Calculated channe final mass (g) 10.3 11.2 14.8 10.5 17.2 12.8 .2 Controlled Variables (same) Dialysis tubing, + time. (final mass-initial mass) initial mass .4 X 100 water % change my group Analysis 1. Calculate the percent change in mass for your solutions. Use the workspace in the data table for help. 2. Graph your data & the class average data. Label the independent (x axis) and dependent variable (y axis). Include a title. After plotting both sets of data one best fit STRAIGHT line. 100 Control The tube filled with water D % change class average 4 .8 46 68 30 1.0

Qualitative Analysis of Carbohydrates HELP Select the test: Glucose, lactose and sucrose are soluble in water, Solubility test whereas starch is insoluble in water. Water Reset Glucose Lactose Sucrose Starch A,

Choose the FALSE statement about protein electrophoresis. The proteins in the gel can be visualized by staining them with silver. The distance and speed that a protein moves depend on its shape. Small proteins move rapidly through the gel. It is performed in a thin, horizontal slab of polyacrylamide. The gel serves as a molecular sieve that enhances separation.

During SDS-PAGE,  the charge on glycine in the separating gel is ____________ while the charge on the protein is _________.     negative; positive     negative; negative     neutral; negative     neutral; positive

Under what pH conditions can a protein not bind to the beads in a column?     pH = -pKa     pH = pI     pH = 7     pH = pKa In size exclusion/gel filtration chromatography, the elution order is dependent upon     Molecular weight     Concentration     Overall Charge     Enzymatic Activity

topic: Determination of Protein Concentration by Spectrophotometry   Enumerate and discuss the limitations of Beer-Lambert’s Law.

Can you please do number 1 and show the steps

Analysis of a protein is taking place. The enzymic acivity of this protein is stable up to temperatures of 40 degrees celsius. ph values are between 2.5 and 11.5.  Now, Ion exchange chromatography is conducted via a software using DEAE-cellulose and method of elution is done by salt gradient. pH is set to 7. In terms of Molar, start of gradient is 0 and end of gradient is 1. The following graph is generated. Using the graph and analytical methods, determine pI of protein.

Qualitative Analysis of Carbohydrates HELP Iodine reacts with starch to form a starch/iodine complex, which gives a characteristic blue colour to the reaction mixture. Glucose, lactose and sucrose do not give this reaction. Select the test: Iodine test A Iodine Solution Reset Glucose Lactose Sucrose Starch

Complete the table below regarding the different laboratory tests done for Amino Acids and Proteins  Tests Procedure (Chemical Reagents Added) Positive Results/ Observations  (ex: color of solution, precipitate formation, etc) Positive for (provide details like functional group responsible) Molisch Test       Benedict’s Test       Barfoed’s Test       Moore’s Test       Bial’s Test       Seliwanoff’s Test       Osazone Test       Fehling’s Test       Tollen’s Test       Mucic Acid Test       Lugol’s Test/ Iodine Test       Hydrolysis w/ Benedict’s Test       Hydrolysis w/ Iodine Test         Provide the expected results with the samples given below:  For negative results just leave it blank, for positive results write “(+) then the expected observation”  ex:  + blue solution   Samples Molisch Test Benedict’s Test Barfoed’s Test Moore’s Test Bial’s Test Seliwanoff’s Test Glucose             Galactose             Fructose             Ribose…

A C2 G This a photograph of an actual polyacrylamide gel that has been run with samples of protein. For each question, write the letter from the item in the gel that best matches the word or concept that is described. Answers may be used once, more than once, or not at all. There may be more than one correct answer per question. 1. Band 2. Lane 3. Well 4. Will protein migrate through the gel from A to B or will it migrate from B to A? 5. Which end is nearest the negative electrode, A or B? 6. Which contains smaller protein fragments, F or G? 7. Which letter indicates the highest concentration of protein fragments that are the same size 8. Where would a sample of protein be loaded? B.

How will you make a series of two-fold dilutions of a protein solution to give 5 different concentrations? The initial concentration of the protein solution is 70ng/μl and the final volume needed (for an experiment) is 10 µl for each dilution.

Which classes of biomolecules would be best separated using normal phase chromatography? Why? steroids mono- and disaccharides flavonoids5.

Mass spectrometry and X-ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to mass spectrometry, X-ray diffraction, or both techniques. Mass spectrometry protein must be conformationally stable X-ray diffraction small amounts of protein are sufficient analysis requires information about the protein-coding gene or genes Answer Bank protein may be denatured requires a large amount of protein protein sample must be pure can detect a covalent modification to a protein Both techniques

If the following lipids are present: phosphatidylserine / phosphatidylcholine / sphingomyelin / triacylglycerol / and cholesterol ester are mixed and the mixture is separated by column technique. chromatography with silica gel in the column and then start Leach with a less polar solvent. The drought gradually increases the polarity of the less polar solvent. and gradually increasing the polarity of the solvent How are the lipids in the mixture in order to emerge from the column? along with explaining the reasons ..

In quantitative determination of protein using spectrophotometer how can I plot the absorbance vs wavelength for the proteins given the transmittance values?

Identify what test is being described: Refers to the breaking of peptide bonds that connect amino acids to compose protein ? Hydrolysis  Denaturation  Heat denaturation  Organic solvent denaturation  Biuret test  Hopkins – Cole Reaction  Millon’s test  Ninhydrin Test  Sulfur test Xanthroproteic Test Chromatography  Paper chromatography  Competitive inhibition Noncompetitive inhibition Rancidity Hydrogenation Identify what test is being described: Test that detects the free amino group in amino acids ? Hydrolysis Denaturation Heat denaturation Organic solvent denaturation Biuret test  Hopkins – Cole Reaction Millon’s test Ninhydrin Test Sulfur test Xanthroproteic Test Chromatography Paper chromatography Competitive inhibition  Noncompetitive inhibition Rancidity Hydrogenation Identify what test is being described: A foreign substance, which is structurally similar to the substrate, competes for the active site of an enzyme ? Hydrolysis Denaturation Heat denaturation Organic solvent…

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Mass spectrometry and X‑ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to mass spectrometry, X‑ray diffraction, or both techniques.