4. Amphiphilic Lipids. Detergents are small amphiphilic molecules that tend to form micelles in water. (a) Draw the structures of sodium dodecyl sulfate (SDS) and Triton X-100 (b) For each drawn detergent, indicate which portions (ends) of the molecules are hydrophilic and hydrophobic. Justify your answer (explain why hydrophilic vs hydrophobic). (c) Draw the micelle structure for one of the detergents. (d) Why does the detergent form a micelle and not a bilayer? Why do detergents denature proteins and remove grease from your clothing?

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).

6. b. Draw a box around the disulfide bridge in oxytocin, if present, or write "none". 7. Mark each peptide bond in oxytocin by making the corresponding line in the structure thicker or marking it with a different color. The first one is shown for you as an example (in dark orange). 8. Number the central carbon of each amino acid in oxytocin by pointing a small arrow to it or by circling the corresponding vertex in the image. Numbers 1 and 2 indicate the central carbons of the first and second amino acids of oxytocin, and are shown for you as an example. 9. Fill out the following table, listing amino acids that make up oxytocin in order, from the N terminus to the C terminus, characterizing each amino acid by the properties of its R group (side chains), and briefly indicating the reasoning for the characterization. You may consult amino acid groupings by category in the slides (or the textbook, p.49), but you must explain the reasoning for each in your own words. CO 1 AA# Abbre- Full…

Compare the stability of the two salt bridges shown circled in blue at pH 8.4. The carboxylate ions are completely de- protonated at pH 8.4 The pka of the amino group (upper left) is 8.1 and the pka of the amino group (bottom right) is 8.7. (d) NH, F-8- Ed (b) O-H- M5 CH₂COOH (c) 5 (b) CH, CH. H--O=C (d) -H H CH,OH (b) KCHJ NH, (a) The bottom right salt bridge is stronger due to the partial positive charge of +2/3. The bottom right salt bridge is stronger due to the partial positive charge of +1/3. The upper left salt bridge is stronger due to the partial positive charge of +1/3. The upper left salt bridge is stronger due to the partial positive charge of +2/3.

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 to

B, C, D, and E please

pls answer the following question

Give detailed Solution with explanation needed (don't give Handwritten answer

biochemistry

4d