Name the protein structural element shown in yellow in the figure:
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- Assume that the 3 polypeptide strands shown below form a parallel B-sheet. Select amino acids AA1, AA2, and AA3 so that the parallel B-sheet is amphipathic and remains stable. Glu-lle-Asn-AA1-Cys-Val Ser-AA2-GIn-Leu-Lys-Phe Lys-Met-Cys-Leu-AA3-Val O AA1 = Pro, AA2 = Leu, AA3 = lle O AA1 = Val, AA2 = Leu, AA3 = Asn O AA1 = Ala, AA2 = Gly, AA3 = Leu AA1 = Phe, AA2 = Arg, AA3 = Ala O OOne of the amino acid sequences in the lysozyme protein from the bacterial virus T4 studiesby Streisinger and co-worker was .... Lys – ser – pro – ser – leu – asn – ala – ala – lys. Thisparticular amino acid was found to have changed to lys – val – his –his –leu –met –ala –ala–lys... as a result of a single nucleotide deletion and addition approximately 15 bases apartin the mRNA. Which base was deleted and which was added? Give the altered sequence of bases inthe altered amino acid.One of the amino acid sequences in the lysozyme protein from the bacterial virus T4 studiesby Streisinger and co-worker was .... Lys – ser – pro – ser – leu – asn – ala – ala – lys. Thisparticular amino acid was found to have changed to lys – val – his –his –leu –met –ala –ala–lys... as a result of a single nucleotide deletion and addition approximately 15 bases apartin the mRNA.a. What is the sequence of the nucleotides that produce the original protein.b. Which base was deleted and which was added? Give the altered sequence of bases inthe altered amino acid.
- Consider the following protein sequence as an α helix: Leu-Lys-Arg-Ile-Val-Asp-Ile-Leu-Ser-Arg-Leu-Phe-Lys-Val. how many turns does this helix make?Like a helices, ß sheets often have one side facing the surface of the protein and one side facing the interior, giving rise to an amphiphilic sheet with one hydrophobic surface and one hydrophilic surface. From the sequences listed below, pick the one that could form a strand in an amphiphilic ß sheet. O TLNISFQMELDV O DSETKNAVFLIL O VLEFMDIASVLDDraw the structure of this peptide: N-Met-His-Tyr-Leu-Asp-Ser-Arg-Leu-C
- Consider the following peptide sequence: Met-Ser-Val-Thr-Ile-Lys-Ala-Cys-Leu-Ser-Ile-Tyr-Phe-Ser Predict if the sequence will fold into an a-helix, ß-strand or not fold. Explain your answer.What is the length in AA’s of the LilP protein? Assume fMet is NOT CLEAVED. Write out the sequence of the polypeptide in AA: use the three letter notation, e.g. Met-Ser-Pro-Each type of molecule listed below is recognized by a specific class of nuclear import receptor (importin) or nuclear export receptor (exportin). For each type of molecule, state whether you think it is recognized by an importin or exportin and explain why (in terms of where that molecule is synthesized, what that molecule does, and where it does it). (a) RNA polyermase II: (b) ribosomal protein: (iii) †RNA:
- a) b) Shown below is a DNA sequence that encodes for a section of a protein. Please write the amino acid sequence using the three letter codes for this section. 5' ATG ACT CTC TCC TGG GGC ATC CGA TAA 3' What would the second codon be changed to if it was both a silent mutation and a transition mutation? Please write an anticodon in 5' to 3' direction that would recognize both the original second codon and the mutated second codon.Shown below are two cartoon views of the small globular protein StrepG inwhich an α helix is packed against a four-strand β sheet. The sheet is madeup of two “β-hairpins” (a β-hairpin is a “β-turn-β” structure). Refer to theimages and answer the questions that follow: (a) Identify the locations of the N- and C-termini of StrepG.(b) Indicate the orientation of the helical macrodipole, showing the (δ+)and (δ-) ends of the macrodipole.(c) How many residues are in the helix?(d) Do you predict that the α helix and β sheet are amphiphilic or not?Briefly explain.(e) The following two peptides are part of the primary sequence of StrepG.Based on your answer to part (d), which one is more likely to correspondto the α helix? Which is most likely to be part of a β-hairpin? Explainyour choice.Peptide #1: DAATAEKVFKQYAND or Peptide #2: VDGEWTYDDATKTFTVGive the effect of the following changes in the protein structure of hemoglobin Replacement of analanine located at the middle of helix B with proline