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- Nearly all bacteria contain peptidoglycan. Review the structure of peptidoglycan by selecting the correct characteristics listed below. Check All That Apply Polymer of alternating N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) Contains a tetrapeptide that extends from N-acetylglucosamine (NAG) Contains D-amino acids not found in proteins All bacteria use a peptide interbridge to connect the sugar strands Peptidoglycan is a strong and rigid structurePlease depict a noncovalent interaction important for the function of lysozyme.Identify the following by describing their functions: EF-G, EF-Tu, EF-Ts, EF-P, and peptidyl transferase
- Place the following steps of the bacterial protein synthesis in their correct order? Peptide bond formation at the peptidyl-transferase center. Binding of MRNA and initiator formyl-methionyl-IRNAMet to the 30S ribosomal subunit, Aminoacylation and formylation of the initiator tRNAMet Joining of the 30S and the 50S ribosomal subunits, Release Factor (RF) dependent hydrolysis of the peptidyl RNA and release of the fully synthesized polypeptide from the ribosome. Elongation Factor G (EF G) dependent translocation of the ribosome by one codon along the MRNA Elongation Factor Tu (EF-Tu) dependent delivery of an aminoacyl-IRNA to the ribosomal A siteList the 4 types of protein modification and describe each in 1 sentenceHere is a putative peptide sequence (position number on top of residues): 1 2 3 4 5 6 7 8 9 10 11 12 13 NH2- G C G N V T H N Q C V L S -COOH If expressed in a eukaryotic cell (please mark your answer in the blank space): Position(s) ___ could be N-glycosylated Position(s) ___ could be modified with myristic acid and the bond formed would be a ______________ Position(s) ______and _____ could be modified with palmiti c acid and the bond formed would be a ______________ Positio n(s) ________ could be a segment of a lipid-linked protein with a farnesyl anchor and the bond formed would be a ______________ Position(s) ________ could be a segment of an O-glycosylated protein Position(s) ________ could be modified with a glycosylphosphatidylinositol (GPI) anchor Position(s) ________ could be phosphorylated
- What to submit: Draw in the hydrogen bonds for parallel and antiparallel sheets and replace the current image with new ones. Underline the correct sheet type. Submit as an image or PDF. Label the amino acids in the following peptide using their three-letter and one letter code H₂N OH Three Letter Code - One Letter Code - ZI IZ ZI NH₂ Draw out the following peptide (CHARLIE) from N to C terminus. Draw by hand and upload as a file attachment. What is the net charge of your peptide? net charge:+Identify if the statement is correct or incorrect, "rRNA serves as template for the synthesis of polypeptide."Protein structure and function: a) Name two common post-translational modifications of proteins in the cell that will affect their structure/function. b) What are prions? Briefly describe their structure and function. C) Explain the principles of protein folding and significance of urea and Bmercaptoethanol in the experimental procedures addressing this question.
- The compartmentalization (division) of eukaryotic cells allows many processes to function properly. Summarize how proteins based on peroxisomal proteins get to the right place.You have isolated this peptide. AÇQGRKSPWTT TAHEVYPGGČMN What products would you get if you treated with: a) DTT ( dithiothreitol) b) Trypsin c) Carboxypeptidase A ( 1 cycle) d) Aminopeptidase M ( 2 cycles) e) DTT, then Iodoacetate, then elastaseWrite the structure formula, three-letter and one-letter abbreviation for each essential amino acid at pH 7. Histidine Arginine Lysine