3.2 In the scheme below, a globular structure of a trans-membrane protein within the cellular membrane is shown. Explain the distribution of amino acids in the core part and on the surface of the globe. FOOW 110 WAO
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- The cell membrane is both fluid and asymmetrical. Discuss asymmetry of the plasma membrane, as well as the enzyme involved. Explain properties that contribute to the fluidity of the cell membrane?1. Glycosphingolipids function via cis regulation and trans recognition. Explain these terms and provide examples of each.In proteins involved in blood clotting to heal a wound, the amino acid GLU is often chemically modified to carboxy-glutamic acid (abbreviated GLA, shown in diagram at pH 7) by a carboxylase enzyme in the blood. The pKa values for the two ionizable protons in the R-group of GLA are shown. A sample of the octopeptide ILE-GLA-ARG-GLY-MET-ARG-PHE-SER was digested with trypsin, adjusted to pH 13, and applied to an anion exchange column. The peptides were then eluted from the column using a pH gradient from 13 to 0.5. Write the order of the products (no structures required) at the pH they would elute from the column and indicate the pH value. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.6 and 2.2 respectively. (Relevant pKa values are 2.2, 3.2, 4.8, 9.6, and 12.5).
- Give the general Adiar equation for the binding of a ligand to a dimeric protein. Explain further what your understanding is of the terms "no-, positive-, and negative cooperativity” and graphically present the relationship between Ȳ and [S] for each of these cases. Also, give the relationship between the constants Kb1 and Kb2 in each case.Of all the high-energy phosphate carriers we've studied in class, PEP has the greatest free energy change associated with the hydrolysis of its phosphate group. Examine the structures of PEP before and after the phosphate is removed, and give a structural explanation for why the free energy change for phosphate removal is so large.68. In animal cells, enzymes synthesized to hydrolyze polymers to form monomers. This process involves the RER, the SER and the Golgi apparatus. In which of the following is the molecule listed for this process employed by the cells of the organ indicated? a) formation of Fatty acids by lipases in the small intestine. b) production of glucose from glycogen by the liver. c) formation of amino acids by proteases in the small intestine d) formation of monosaccharides by Carboxylases in the mouth and small intestine. e) all are possible
- Myoglobin stores O2 in muscle tissue to be used by the mitochondria only when the cell is in oxygen debt, whereas hemoglobin can effectively transport O2 from the lungs and deliver it discriminately to cells in need of O2. Describe the structural features that allow these two proteins to accomplish separate functions.The process of a protein folding from an inactive unfolded structure to theactive folded structure can be represented by the following equation: unfolded protein ⇌ folded proteinThe values of ΔH° and ΔS° for the folding of the protein lysozyme are: ΔH ° = -280 kJ/ mol ΔS ° = -790 J/mol • K(a) Calculate the value of ΔG° for the folding of lysozyme at 25 °C.(b) At what temperature would you expect the unfolding of lysozyme tobecome favorable? (c) At what temperature would the ratio of unfolded protein to foldedprotein be 1:5?Give the molecular basis of the observed mechanical properties of glutenin, a wheat storage protein rich in disulfide linkagesand responsible for the cohesive and elastic characteristics of dough made from wheat flour. Use not more than 10 short sentences for this item.
- Assume that a new oxygen transport protein has been discovered in certaininvertebrate animals. X-ray diffraction of the deoxy protein reveals that ithas the dimeric structure shown in panel (a) of the accompanying figure,with a salt bridge between residues histidine 13 and aspartic acid 85. Thetwo monomers interact by salt bridges between the C- and N-termini. TheO2-binding site lies between the two iron atoms shown, which are rigidlylinked to helices A and C (see panel (b)). In the deoxy form, the spacebetween the iron atoms is too small to hold O2, and so the Fe atoms must be forced apart when O2 is bound.Answer the following questions, explaining your answer in each case interms of the structure shown below.(a) Is this molecule likely to show cooperative oxygen binding?(b) Is this molecule likely to exhibit a Bohr effect?(c) Predict the likely effect of a mutation that replaced aspartic acid 85 bya lysine residue.Do you think that the Ea for ATP hydrolysis is relatively low or high? Explain your reasoning.Chondroitin sulfate chains have been likened to a large fishnet, allowing small molecules to pass through but excluding large ones. What structural features of chondroitin sulfate and proteoglycans in general are responsible for this phenomenon?
