Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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- 6. A control phospholipid membrane is isolated in which the phospholipid tails all have an 18-C chain length and are comprised of a 50:50 mixture of saturated and unsaturated tails. In addition, about 25% of the lipids are fluorescently labeled on the head groups. a) Draw a single plot of Fluidity vs. Temperature that contains the expected curves for: Control phospholipid (line- -) Control supplemented with 18-C saturated phospholipids (dashed line - Control supplemented with 16-C chain length (dotted line • • • • • • ) b) Draw a single plot of the Fluorescence Intensity vs. Time that contains the expected curves of a Fluorescence Recovery After Photobleaching (FRAP) using the same samples as in (a) above. The FRAP experiment is conducted at the same temperature for each sample (which is the Tm of the of the control phospholipid).arrow_forward17. Protein folding results in a large decrease in entropy since a polypeptide is now constrained and more ordered. However, what counterbalances the loss of entropy associated with protein folding?arrow_forward1. Theoretically, a protein could assume a virtually infinite number of configurations and conformations. Suggestseveral features of proteins that drastically limit the actual number. 2. What are the greatest structural features that differentiate sphingolipids from phosphoglycerides? 3. High levels of glucose-6-phosphate inhibit glycolysis. If the concentration of glucose-6-phosphate decreases,activity is restored. Why?arrow_forward
- Select two molecules that could be found in a protein, and from the two molecules, are they lower or higher numbered amino acids and would they be acidic, basic, polar, or nonpolar?arrow_forwardDraw beta sheet with backbone hydrogen bonds, is this structure on the interior or exterior of the protein and why? Region 1: -Ser-Thr-Glu-His- Region 2: -Asp-Tyr-Lys-Asnarrow_forward3. The figure below depicts a protein folding into its final shape. If this was a cytoplasmic protein: goa oog ge Tertiary Structure a. The chemical properties of the amino acids in black are likely (circle): Polar or Nonpolar Primary Structure b. The chemical properties of the amino acids in white are likely (circle): Polar or Nonpolararrow_forward
- 3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of moleculearrow_forward2. Identify the structural level in each protein. A) quaternary structure B) tertiary structure C) secondary structure D) primary structure 1) The protein folds into a compact structure stabilized by interactions between R groups. 2) the combination of two or more protein molecules to form an active protein 3) B-pleated sheet 4) the peptide bonds betwecen the amino acids 5) the structural level achieved when hydrogen bonds form between the carboxyl group of one amino acid and the amino group of a different amino acidarrow_forward1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic point of the amino acids are as follows: histidine:7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.arrow_forward
- 1. Is there more than one way to fold a protein, given the conflicting demands of the different "R" groups and the protein existing in a watery environment? 2. Explain what an R group is. 3. Compare the backbone of a polypeptide with that of a nucleic acid. 4. Proteins perform critical functions in all of our cells. Without proteins, life wouldn’t exist. Think of some specific proteins and describe what function they perform. 5. Explain the difference between secondary and tertiary protein structures.arrow_forward4.) If a mutation in an organisms DNA causes the resulting protein to possess an alanine residue to be in the 13th position instead of a glycine, what level(s) of the resulting protein's structure would likely be affected? Why? Why would the other(s) not be affected? 14:arrow_forwardIt is observed that as temperature is increased, most protein molecules gofrom their defined, folded state into a random-coil, denatured state thatexposes more hydrophobic surface area than is exposed in the folded state.(a) Given what you have learned so far about ΔH and ΔS, explain why thisis reasonable. (b) Sometimes, however, proteins denature as temperature is decreased.How might this be explained?arrow_forward
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