anslucent liquid, coritaining olded protein. In the next part of the lab youiw i
ID: 1029483 • Letter: A
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anslucent liquid, coritaining olded protein. In the next part of the lab youiw investigate the conditions that can ture (unfold) a protein. s. Investigating Protein Stability. prepare a reference standard. To do this, label a small test tube as 'standard. Then, add of your protein solution to 5.0mL of 0.10 M sodium phosphate buffer, pH 7.0 As you continue to test the stability of the protein under various conditions, you can compare samples to this standard, to judge whether the protein appears to be misfolded. 9 ) 1. Stability of the protein at various pH values a) Label 4 test tubes with "2", "4", "7 and *10 b) To each, add 1.0mL of the protein solution, followed by 5.0mL of buffer c) Mix well, wait approximately 5 minutes, and compare each of the samples to the reference at the appropriate pH. standard. Record your observations in Data Table 1. DATA TABLE 1 Describe your observations: Color of solution? Protein folded or unfolded? PH Precipitation? Fluorescence? cioudy, Iigni biue, no fluorenscence 2 unfolded Precipianión sigmibt cloudy hgni blue unfoldeq NO IUorescnce 7 Dar blve, ranspoveni Re FluoresCensce folde d 10 ie Faded in coior nghi bive noi Guile ign bhe - trans paven folded ense 2. Stability of the protein at various temperatures Create four water baths at four different temperatures-an ice water bath, a 25°C water bath, a 60°C water bath and boiling water bath. Use a thermometer to record the exact temperature of each water bath for Data Table 2 Dilute 4.0 mL of your protein with 20mL of 0.100 M sodium phosphate buffer, pH 7.0. Mix well, then divide this dilution equally between 4 test tubes. Label these tubes with the temperature of each water bath a) b) Page 3 of5 AC/KB F16 Chem&131LExplanation / Answer
Answer .
1. Optimal pH range for protein stability is 2 to 4.
2. IMF between define+asparagine = hydrogen bond
Leucine+alanine D lysine+ aspartate vander wall bond.
3. And 4 At pH 7 both lysine and aspartate has normal structure.
4. Arginine and lysine can be destabilized at low pH.
5. Aspartic and glutamic amino acids can be destabilized at high pH.
6. As part if acid will be affected due to neutral to basicpH.
7. The optimal range for this practical data protein is 80 to 100 degree Celsius.
8. First boil for 20 min then cool slowly and finally freeze to avoid bacterial degradation.
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