The structure shown below belongs to which family of protein tertiary structure? 1) x/B barrel 2) B-barrel 3) x-helix bundle 4) xß-sandwich PDB: 1VRD
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- The structure shown below belongs to which family of protein tertiary structure? PDB: 1Z4A 1) a/ß barrel 2) B-barrel 3) a-helix bundle 4) aß-sandwichFor the three peptides below, label whether they would form an amphiphilic beta-strand, amphiphilic helix, or nothing. Explain why. Part a) S-V-K-I-Q-M-R-A-D-L Part b) A-L-E-H-M-F-R-Y-L-A-K Part c) A-L-A-I-W-F-P-D-R-K-EA sequence of amino acids in a certain protein is found to be -Ser-Gly-Pro-Gly-. The sequence is most probably part of a(n): A) parallel β sheet. B) α sheet. C) β turn. D) α helix. E) antiparallel β sheet.
- What is the CORRECT way to classify the protein below according to its secondary- structure elements? un a) not possible to determine b) all a ○ c) alẞ Od) a + B e) all BConsider the sequences (i-iv) that represent sections of a protein. ) -АЕEAAAAMAАAАMAAY ii) -KVIVVVTVVTVVVKVV- iii) -GPPGPPGPPGPPGPPGPP- iv) -WYFWYFWYFVVFFFVV- Which of the following statements is likely to be true? O Sequence (iv) is likely to have an alpha-helix structure. O Sequence (i) is likely to have an alpha-helix structure and sequences (i) and (iv) are most likely to have beta- sheet structures O Sequence (ii) is ikely to be a metal-binding domain. O Sequence (i) is likely to have a beta-sheet structure and sequences (ii) and (iv) are most likely to have alpha- helix structures O Sequence (ii) is most likely have a beta sheet structure with a hairpin turn.A peptide with the sequence isoleucine1-aspartate2-valine3-lysine4-proline5-glutamate6 is located at the surface of a protein. Which residues are likely oriented toward the interior of the protein and what is the most likely secondary structure that this peptide is in? a.) Residue numbers 2, 4, 6; alpha helix b.) Residue numbers 1, 3, 5; alpha helix c.) Residue numbers 1, 3, 5; beta sheet d.) Residue numbers 2, 4, 6; beta sheet
- Consider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary)as defined for proteins.(a) What level is shown by double-stranded DNA?(b) What level is shown by tRNA?(c) What level is shown by mRNA?Consider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary) as defined for proteins. (a) What level is shown by doublestranded DNA? (b) What level is shown by tRNA? (c) What level is shown by mRNA?A protein contains three 60-kD polypeptides and six 20-kD polypeptides. Each 60-kD chain is disulfide bonded to two 20-kD chains. The 100-kD units associate noncovalently to form a protein with a molecular mass of 300 kD. Which of the following is correct? a) PAGE shows one single band b) Molecular masses determined by SDS-PAGE with 2-mercaptoethanol are 20kD and 60 kD c) Molecular mass determined by gel filtration is 300 kD d) All answers are correct e) Molecular mass determined by SDS-PAGE without 2-mercaptoethanol is 100 kD can you explain the steps and calculations to solve this question?
- The R group or side chain of the amino acid serine is -CH2-OH. The R group or side chain of the amino acid leucine is -CH2-CH-(CH3)2. Where would you expect to find these amino acids in a globular protein in aqueous solution ?A) Both serine and leucine would be on the exterior of the globular protein. B) Both serine and leucine would be in the interior and on the exterior of the globular protein. C) Serine would be in the interior, and leucine would be on the exterior of the globular protein. D) Both serine and leucine would be in the interior of the globular protein. E) Leucine would be in the interior, and serine would be on the exterior of the globular protein.Which of the following is primarily responsible for stabilizing the a-helix, a type of 1. secondary structure formed by a single nolvpeptide chain? hydrophobic interactions hydrogen bonds of backbone ionic interactions disulfide bridges hydrogen bonds involving the R-side chains a) b) atoms d) The atoms that make up the peptide bond that links amino acids together in a protein are in the same plane (coplanar). In the a-helix, how are these peptide bond planes arranged? 2. a) perpendicular to the a-helix approximately parallel to a-helix axis b) both parallel and perpendicular to the a-helix randomly oriented with respect to the axis of the a-helix peptide bond planes don't exist in the a-helixConsider protein folding that results when the following components interact: Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups. Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.