This review sheet will be “graded” for completeness, meaning that you earn 5points for submitting it on Moodle bySunday night. The answer key is already posted on Moodle, so you can check your answers after you complete it. This reviewdoes not cover everything that will be on the test and some things covered in this review may not be on the test.1. Which of the following can NOT easily diffuse through a phospholipid bilayer? Select all the apply. Explain why.a. H+ (hydrogen ions) - charged ions wouldn’t be able to easily diffuseb. Sugars - large and not easily diffusible, slow ratec. Sodium ions - charged, can’t diffused. O2 (only one that can easily diffuse)e. ATP - phosphates are chargedf. A protein made up of many serines and glutamines - proteins are too large to diffuse1. True or false regarding the lac operon. In the lac operon, when both glucose and lactose are present in highconcentrations you would expect to find (select true or false for each of the following statements).● High levels of CAP – cAMP bound at the positive control binding site on the DNA. F● The repressor protein would be bound at the operator site. F● The lacI would not be expressed because of the high lactose concentrations F● RNA polymerase would be bound to the promoter and would be actively transcribing the lacZ and lacY genes. T1. How many molecules of water were produced from the reactions that created this polypeptide? (2 H20 molecules)1. Explain what would happen to lacZ and lacY expression if there were a mutation in the operator site such that therepressor protein was unable to bind under the following sets of conditions:a. High lactose, low glucose - High rates of gene expressionb. No lactose, high glucose - slower expression of gene expression1. The sequence below shows part of an mRNA transcript, the start codon is not shown (but it exists). Where would youexpect this section of the protein to be located in a cytosolic protein? Explain you answer in 1-2 sentences.5’-CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC-3’(Nonpolar, on the inside)1. True or false – regarding protein folding.● Arginine, at physiological pH (that is, normal) can participate in ionic bonding with either glutamic acid or asparticacid. T● Threonine and serine can form hydrogen bonds with one another or water molecules. T● Only polar amino acids can be in an alpha helix because hydrogen bonds hold secondary structure together. F1. First transcribe, then translate the coding sequence below. Assume the frame begin with the first codon. Then create amutation that leads to a negative charge increase on this peptide while decreasing its hydrophobicity. Decide what tomutate and show how it would change the DNA sequence and the protein sequence.Template: 5’ GGT-CCT-CAC-AGC-CAT-3’Transcription: 5’ - AUG- GCU- GUG- AGG- ACC- 3’Translation: Met- Ala- Val- Arg- ThrMutant Protein: Met- Asp- Val- Arg- ThrMutant DNA: 5’ GGT- CCT-CAC- UAG- CAT-3’1. This is the overall reaction for photosynthesis. We can estimate that ΔG = 686 kcal/mol6CO2+ 6H2O ⎯⎯→C6H12O6+ 6O2a. If you mixed the reactants in a test tube, would this reaction occur spontaneously? Explain your answer in 1-2sentences. No, it wouldn’t occur spontaneously, but it would happen with energy.b. Is there more free energy in the reactants or the products? Products.Read the following information about protein folding and Alzheimer’s. Then answer the questions.Alzheimer's disease is a chronic neurodegenerative disease that usually starts slowly and worsens over time. People withAlzheimer's experience memory loss and impairments to other important mental functions. Most Alzheimer’s occurs in theelderly, but about 1/2 million of the 5 million people who develop dementia or Alzheimer’s each year are under 65.Approximately 5% of Alzheimer’s is caused by inherited dominant mutations. People with the mutation develop symptoms muchearlier than typical (~age 51). Some of these mutations are changes in the amino acids in the ß-APP protein. The biology andbiochemistry of Alzheimer’s disease is still not well understood and there is a lot of current research focused on finding the causeof, and treatments for, Alzheimer’s disease.ßAPP, ß-amyloids, and Alzheimer’s diseaseß-amyloid precursor protein (ßAPP) is a large membrane protein that normally plays an essential role in neural growth and repair.It is found in nerve cells (neurons). It is 695 amino acid long. ß-amyloids are ßAPP fragments that are composed of 28 aminoacids.Ubiquitin-mediated proteolysis marks proteins for destruction by first tagging the protein with ubiquitin and then proteases(enzymes that break peptide bonds by hydrolysis) break down the tagged protein into amino acids. This process removes proteinswhen they are no longer needed. ß-amyloids are small fragments of ßAPP. Plaques form when ß-amyloids clump together.ß-amyloids are chemically "sticky", the fragments stick together and gradually builds up into plaques. These plaques damagenerve cells, which may explain the memory damage associated with Alzheimer's.1. Compare these two peptide sequences, how are the two polypeptides different?There is a PHE inserted for the His in the mutant.β-amyloid: Asp-Ala-Glu-Phe-Arg-His-His-Ser-Gly-Tyr-Glu-Val-His-HisMutant β-amyloid : Asp-Ala-Glu-Phe-Arg-His-Phe-Ser-Gly-Tyr-Glu-Val-His-Hisa. What level of protein structure is shown above?Primary protein structure.1. Unmutated and mutant β-amyloid have very different shapes. Why could changing one amino acid cause the wholeprotein to change shape?The proteins would not be able to form the same way, with some being hydrophobic instead of hydrophilic.1. ßAPP is transmembrane protein. List 2 amino acids which you would expect to find in the intra-membrane region ofthis protein (facing the fatty acid tails of the plasma membrane). List 2 amino acids which you would expect to find inthe extracellular facing region of this protein.Leucine, isoleucine.1. Mutant β-amyloids have the amino acid phenylalanine at position 717 rather than histidine. Mutant ß-amyloidfragments stick together which causes plaques to form which can lead to Alzheimer’s. Explain why a mutation thatchanges histidine to phenylalanine may cause plaques to form more easily.Instead of having the charged histadine, it is replaced with non-polar phenylalanine. Phenylalanine will clump togetherother hydrophobic amino acids.1. The following bonds are