In a sequence of amino acids, a non-polar amino acid is mutated into a polar charged amino acid. Which of the following describes what levels of protein strucutures/folding is affected by this mutation? Primary, secondary, tertiary, quaternary Secondary, tertiary, quaternary Primary, Secondary, Tertiary Primary, Secondary
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- Mutations in proteins do not always lead to a drastic effect on a protein's function. Substitutions that can maintain the physical and/or chemical characteristics of a protein can happen without any noticeable effect on a protein's characteristic. In the protein sequence below, the amino acid residue in red was shown to be essential to the function of the protein. .AAVILGLIFFFLVIVIVAL. If this residue was to be replaced by another, which of the following replacements would most likely lead to an abrogation of the protein's function? OD OV O AWhich of the following describes the most likely outcome of a mutation that causes a sin- gle amino acid to be removed from a protein subunit? A It will affect the primary, secondary, and tertiary structures of the protein. B с D It will affect the secondary and tertiary structures of the protein but not the primary structure. There will be no observable effect on the structure of the protein. It will change the primary structure of the protein without affecting other structures in the protein.In the amino acid sequence below, the amino acid residue in red was shown to be essential to the function of the protein. .VAIALWLIFWFIISVGGIY. If this residue was to be replaced by another, which of the following replacements would most likely lead to an abrogation of the protein's function? OL O E OG O A
- When an inappropriate amino acid is substituted in place of another, as occurs in certain genetic disorders, the resulting protein is either poorly functional or non-functional. Since proteins contain hundreds if not thousands of amino acids, why should the change of a single amino acid be so critical?At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? A mutation in the genetic sequence, which ultimately causes an amino acid to change(e.g. Trp – Asn – His turns into Trp – Arg – His) Dissolving a protein in a non-polar solvent (like oil) instead of water.Which of the following statements best describes the hydrophobic character of bacteriorhodopsin (2BRD)? Both the interior and exterior of the protein are hydrophobic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, but the central core of the trimer is hydrophobic. Both the interior and exterior of the protein are hydrophobic, but the central core of the trimer is hydrophilic.
- What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.Which of the following about the glycosylation of proteins in the ER is false? Dolichol phosphate serves as a lipid carrier. Oligosaccaryltransferase add the oligosaccharide to the protein. The oligosaccharide ‘tree’ is made up of glucose and mannose. Asn-X-Ser/Thr serves as the glycosylation site on the protein. Carbohydrates are added to the lipid carrier by glycosyltransferases.It is often the case that a helices are positioned in a protein such that one side faces the interior of the protein and the other, the surface of the protein. These are said to be amphiphilic helices because they face different environments. Using a helical wheel projection (shown below), which of the peptide(s) below might form an amphiphilic helix? 8 15 1 12 4 11 16 18 9 7 14 13 10 17 O SLIKSVIEMVDEWFRTFL O FLIRVLRKVFRVLTRILS O RLFRSRVLKIAVIRFLLI
- List two types of DNA mutations and state which one is more likely to have a severe effect on the resulting protein structure and function. Please explain in 5 sentences or less, thank you!Which of the following statements are true? The local folding of the polypeptide in some regions gives rise to the secondary structure of the protein. The most common secondary structures are the α-helix and β-pleated sheet structures. Certain amino acids have a propensity to form an α-helix, while others have a propensity to form a β-pleated sheet. Select the correct answer below: 1 and 2 1 and 3 2 and 3 all of the aboveDescribe why this position in your protein is important and outline the effects the mutation will have on the 3D structure and the function of your protein. (up to 50 words) My PDB code: 3GRS Residue point: HIS 467 Mutation: LEU 467