Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Textbook Question
Chapter 31, Problem 3P
Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
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Student Guide (continued)
Record data and conclusions about the mystery food sample either below or in a lab notebook.
Step 2: Protein Test (Biuret Solution)
Gelatin
Water
[Mystery Food
(Positive Control)
(Negative Control)
Sample
pink purple
no change
no change
They mystery food sample does not contain protein because the color of the
test tube wasn't pink or purple
Color
Conclusion They mystery food sample does not contain protein because the color of the test tube
wasn't pink or purple
Step 3: Lipid Test (Sudan Red Solution)
Vegetable Oil
Water
(Positive Control)
(Negative Control)
Mystery Food
Sample
floating red
no change
floating red
the mystery food dosnt contain lipids because the test tube has floating red
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The rate data from an enzyme catalyzed reaction with and without an inhibitor present is found in the image.
Question: what is the KM and Vm and the nature of inhibition
1. Estimate the concentration of an enzyme within a living cell. Assume that:
(a): fresh tissue is 80% water and all of it is intracellular
(b): the total soluble protein represents 15% of the weight
(c): all the soluble proteins are enzymes
(d): the average molecular weight of the proteins is 150,000
(E): about 100 different enzymes are present
please help I am lost
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- The following data were recorded for the enzyme catalyzed conversion of S -> P Question: what would the rate be at 5.0 x 10-5 M [S] and the enzyme concentration was doubled? Also, the rate given in the table is from product accumulation after 10 minuets of reaction time. Verify these rates represent a true initial rate (less than 5% turnover). Please helparrow_forwardThe following data was obtained on isocitrate lyase from an algal species. Identify the reaction catalyzed by this enzyme, deduce the KM and Vmax , and determine the nature of the inhibition by oxaloacetate. Please helparrow_forwardIn the table below, there are sketches of four crystals made of positively-charged cations and negatively-charged anions. Rank these crystals in decreasing order of stability (or equivalently increasing order of energy). That is, select "1" below the most stable (lowest energy) crystal. Select "2" below the next most stable (next lowest energy) crystal, and so forth. A B 鹽 (Choose one) +2 C +2 +2 (Choose one) D 鹽雞 (Choose one) (Choose one)arrow_forward
- 1. Draw the structures for the fats A. 16:2: w-3 and B. 18:3:49,12,15 2. Name each of the molecules below (image attached)arrow_forwarddraw the structures for the fats A. 16:2:w-3 B 18:3:9,12,15arrow_forward1. Below is a template strand of DNA. Show the mRNA and protein that would result. label the ends of the molecules ( refer to attached image)arrow_forward
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