The peptide below is placed into a buffer with a pH = 9.1 H₂N-CH-C- -NH–CH—CNHCHC NH–CH CH3 HỌ-CH, CH₂ CH₂ CH₂ H₂C HN-CNH, NH₂ CH₂ CH CH3 -C What direction will the peptide move? If it will move towards the positive electrode give your answer as 1 If it will move towards the negative electrode give your answer as -1 If it will not move give your answer as 0 NH–CH- -C-OH CH₂ -OH
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Give typed explanation
![The peptide below is placed into a buffer with a pH = 9.1
i
H3N-CH-C- -NH–CH-CNH-CH-C-
CH3
CH₂
CH₂
CH₂
H₂C
HN-C=NH,
NH₂
CH₂
CH
CH3
NH—CH_{
HỌ-CH,
NH–CH C-OH
CH₂
1862
What direction will the peptide move?
If it will move towards the positive electrode give your answer as 1
If it will move towards the negative electrode give your answer as -1
If it will not move give your answer as 0
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- Which of these compounds is most soluble in water at pH 7.0? (Note that the non- ionized forms are shown, and remember that ionization will impact solubility!) ( CH3-CH2-CH2-CH2-NH2 CH3-CH₂-CH₂-CH₂-CH3 O CH3-CH2-CH2-CH2-CHO OCH3-CH₂-HCO-O-CH3 (an ester)A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, and phosphatidylcholine was applied to a hydrophobic interaction chromatography column. The column was washed with a high salt buffer and the lipids were eluted with decreasing salt concentrations. In what order would the lipids be eluted from the column? Explain your answer.A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, and phosphatidylcholine was applied to a hydrophobic interaction chromatography column. The column was then washed with increasingly nonpolar solvents. IWhat order would the lipids be eluted from the column?
- A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, phosphatidylserine, andphosphatidylethanolamine was applied to a hydrophobic interaction chromatography column. Thecolumn was washed with a high salt buffer, and the lipids were then eluted with decreasing saltconcentrations. In what order would the lipids be eluted from the column? Explain your answer.What is the charge on the following peptide at standard biochemical pH? S-Y-D-F-K-I-V-F-L-L +2 -1 0 0 0-2 O +1Given below are sequences of amino acids present in an oligo-peptide chain. Count the overall chargeof each assigned peptide and write it in your answer. Along with it also mention that toward swhichelectrode (cathode or anode) will the peptide move? Please remember that cathode is a negativeelectrode and anode is a positive electrode. Ile-Lys-Arg-Trp-Lys-Asn-Glu-His-Pro-Asp-Ala-Tyr-Phe-Glu-Met-Phe-Gly-Val
- ok-Personal Microsoft Edge com/maildeeplink 021 pdt Download Print Save to OneDrive 1. Draw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in aqueous solution at pH3D10.3. (Relevant pka values are: 2.2 4.3, 6.0, 9.8, and 10.1) Acp is adiusted toGiven below are sequences of amino acids present in an oligo-peptide chain. Count the overall charge of each assigned peptide and write it in your answer. Along with it also mention that toward which electrode (cathode or anode) will the peptide move? Please remember that cathode is a negativeelectrode and anode is a positive electrode. Ile-Lys-Arg-Trp-Lys-Asn-Glu-His-Pro-Asp-Ala-Tyr-Phe-Glu-Met-Phe-Gly-ValWhat will be the result for each qualitative test if the intact casein contains the following peptide chain: Ala-Arg-Asp-Glu-Gly-His-Ile-Leu-Lys-Met-Phe-Pro-Ser-Thr-Trp-Tyr-Val What will be the result for each qualitative test if hydrolysis of casein results to the following: Acid hydrolysis = Total hydrolysis of peptide bonds; Trp is destroyed and converted to humin (black pigment); Thr and Ser are destroyed; Asn and Gln are converted to Asp and Glu Basic hydrolysis = Total hydrolysis of peptide bonds; promotes racemization; Thr and Cys are lost; Arg is destroyed
- 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 0.007A mixture of proteins contains Pepsinogen (35 kDa), Fumarase (49 kDa), Transferrin (80 kDa) and Thyroglobulin (340 kDa). Rank these proteins based on the order of their elution from a gel filtration column (1 being the first one to elute and 4 as the last one). Throglobulin Pepsinogen Fumarase TransferrinThe following peptides were separated using ion-exchange chromatography based on the use of an anion exchange resin. Which peptide was eluted first? A B Peptide Name A B C D Molecular Weight (g/mol) 360 1080 1800 1440 Peptide Net Charge -2 -1 0 +1