Activity of a protein as a function of pH 100 Percent activity (%) 8 50 55 60 6.5 7.0 75 80 8.5 PH
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Need help, please. Based on the inserted curve, if this enzyme was Chymotrypsin, please explain how this behavior could make sense.
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- Does this calculation look correct? My goal isto have a target mass of 10 µg of my protein with a total volume of 30 µl. Protein was measured and found to have a concentration of at 308.35 µg/ml Recall, mass = concentration * volume 10 µg = 308.35 µg/ml * V V = 0.01 mg/ 0.30835 mg/mL = 0.032430679 mL = 32.43067942 µL Note: cannot measure this amount; two dilutions required. Dilute by 1/40: measure 2.5 µl of protein at 0.30835 µg/µl and add it to 97.5 diluent to prepare a solution of protein at 7.71 mg/ml. This diluted sample will be used further. Mass = concentration * volume 10 µg = 7.71 mg/ml * V V = 0.01 mg/ 7.71 mg/ml = 1.3 µL Therefore, will measure 1.3 µl of protein at 7.71 mg/ml and add it to 28.7 µl of diluent.Quantitative Estimation of Amino Acids by Ninhydrin http://vlab.amrita.edu/?sub=3&brch=63&sim=156&cnt=2 can u help me with question 2 of the assignment questions Based on the experimental data provided, estimate the amount of amino acid in the given unknown solution by Ninhydrin method. SI No. Volume of standard amino acid solution (ml) Amount of amino acid (µg) OD at 570nm 1 Blank 0 2 0.2 0.12 3 0.4 0.25 4 0.6 0.45 5 0.8 0.55 6 1.0 100 0.68 7 Unknown (0.5ml) 0.41Given: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?
- Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Мyoglobin 7.0 16.7 What is the appearance after visualization of a protein mixture containing the seven proteins above when subjected to SDS-PAGE?TABLE 3-1 Properties and Conventions Associated with the Amino Acids pk, values Amino acid Phenylalanine Tyrosine Tryptophan 5.66 5.48 9.59 5.89 Abbreviation/ symbol 6.14 Phe F Tyr Y Trp W pk, M, (-COOH) 165 181 204 . 1.83 2.20 2.38 Using the table 3-1, calculate the pl of Tyrosine. Hint: Consider the structure and overall charge of the molecule between each pka. pK₂2 (-NH) 9.13 9.11 9.39 PKR (R group) 10.07Materials - 2021FA-CHM-1O X Bb 4427577 d-fleet02-xythos.content.blackboardcdn.com/6086c260d7e8f/4427577?X-Blackboard-Expiration=1633143600000&X-Blackboard-Sig 6 / 9 100% Exercise 1: Standard Curve for Protein Measurements: A standard curve for protein concentration is often created using known concentrations of bovine serum albumin (protein). This process is called the Bradford Assay; it is a colorimetric assay. A special reagent turns blue when it binds to amino acids present in protein. The intensity of the color is best measured with a spectrophotometer (a device for comparing two light radiations, wavelength by wavelength). In the case of the Bradford Assay the greater the absorbance, the higher the protein concentration. A series of tests were performed on some samples and spectrophotometer: following measurements were obtained using a Protein Concentration (mg/ml) Absorbance (A) 0.26 0.098 0.56 0.213 0.383 0.84 1.12 0.473 1.40 0.527 TASKS: 1. Enter the data into Excel - the…
- 5/ n SO a- 6.46 The following data show the binding of Mg2+ ions with a protein containing n equivalent sites: [Mg2+ ] total/μM [Mg2+ ]free/μM 108 Com 35 180 65 288 501 115 248 752 446 Apply the Scatchard plot to determine n and Ka. The protein concentration is 98 µM.Denaturation of Proteins The following are four levels of protein structures. Identify the inter- and intramolecular forces of attractions that stabilized each level. Level of Protein Structure Forces of Attraction Present Primary Secondary Tertiary Quaternary 2.) What is denaturation? 3.) What are denaturing agents? Give three examples and describe their effects on protein. 4.) Differentiate reversible and irreversible denaturation. 5.)Why is 70% ethanol is more effective than 100% ethanol to kill bacteria?1.0 0.9 Z 0.8 15. A pharmaceutical company studied the binding of three different compounds, X, Y, and Z, to a particular protein of interest. For each compound, the fractional saturation (v) was determined as a function of concentration. The results are shown in the figure. Which of the three compounds has the strongest affinity for the protein? Explain. 0.7 X 0.6 > 0.5 0.4 0.3 0.2 0.1 0.0 Y 0.0 0.2 0.4 0.6 0.8 1.0 1.2 1.4 1.6 1.8 2.0 2.2 2.4 2.6 2.8 3.0 L(μM)
- 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 +1The isoelectric point, pI, of the protein deoxyribonuclease I is 10.2 , while that of pepsin is 1. What is the net charge of deoxyribonuclease I at pH 7.3 ? What is the net charge of pepsin at pH 3.5 ? The isoelectric point of tryptophan is 5.89 ; phenylalanine , 5.48 . During paper electrophoresis at pH 6.5 , toward which clectrode does tryptophan migrate? During paper electrophoresis at pH 4.5, toward which electrode does phenylalanine migrate? [Amino acids are not stored in the body. Describe how excess amino acids are processed in the cell.