Look at the m-RNA message below: PUT A NUMBER under each of the t-RNA/amino acid complexes to show the correct sequence that they would attach as this message is read. methionine AUGUUCAA ACUG UUU UA MRNA WHAT IS THE AMINO ACID SEQUENCE FOR THE PROTEIN THAT WOULD BE PRODUCED FROM THIS MESSAGE? MATCH THE PARTS IN THE DIAGRAM WITH THE CORRECT LABEL. RIBOSOME Asparagine D. NUCLEUS Methionine G. MESSENGER RNA ANTICODON Fodiln E 10010000nn AMINO ACID CODON TRANSFER RNA
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- Suggest which part of this sequence belongs to the inner part of the protein and which to the outer shell (use the one-letter code to define amino acid. 1 letter - 1 amino acid): MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEOQWF TEDPGPDEAPRMPEAAPPGVAPTYSAOn average, how many phosphoanhydride bonds (P;-P; bonds) are directly hydrolyzed in thecourse of synthesizing a 200 amino acid protein? Assume that you begin with the mature mRNA,ribosomal subunits, tRNAs, free amino acids, and all necessary factors.For the peptide Ala-Cys-His-Ile-Leu-Asp a. Write the single letter code for the amino acid residues b. What is the charge of the peptide at pH 7.0. Assign the following pKa values: 3,4,6,8,9 c. What is the pI of the peptide
- Remembering that the amino acid side chains projecting from each polypeptide backbone in a β sheet point alternately above and below the plane of the sheet, consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg- Leu-Lys-Ile-Arg-Phe-Glu. Do you find anything remarkable about the arrangement of the amino acids in this sequence when incorporated into a β sheet? Can you make any predictions as to how the β sheet might be arranged in a protein?=Suggest, which part of these sequence referred to inner core of the protein/ outer core (use single letter code to determine the amino acid. 1 letter - 1 amino acid): MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDP GPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSG 1. TAIn the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe- Ser-Gin-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys The hydrophobic residues in this sequence are presented in boldface type. Use helix wheel to demonstrate this peptide is an amphipathic helix.
- N. HN H3N Where on this amino acid does it attach to a primary sequence of a protein and where is the ionizable position of the R group?Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. [References] If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced by another amino group, what would be the predominant form of this amino acid at pH 12 if the pK, value were 10 for the unique amino group? (Select all that apply.) Both of the carboxyl groups are deprotonated. The amino acid-carries a negative 2 charge. The amino acid carries a negative 4 charge. The amino groups are in the form -NH". Both of the amino groups are deprotonated.Translate the given amino acid sequence into one-letter code. Glu-Leu-Val-Ile-Ser-Ile-Ser-Leu-Ile-Val-Ile-Asn-Gly-Ile-Asn-Ala-Thr-Leu-Ala-Asn-Thr-Ala Translated code: X Incorrect
- Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?A peptide with the primary structure Lys-Arg-Pro-Leu-Ile-Asp-Gly-Ala must be synthesized by the methods developed by Merrifield. Calculate the percentage of the peptides synthesized that will be full length and have the correct sequence if the addition of each amino acid residue is 96% efficient. Do the calculation a second time but assume a 99% efficiency for each cycle. full-length peptides with the correct sequence if 96% efficient: full-length peptides with the correct sequence if 99% efficient: % %Which of the following peptides will likely form a loop or turn in a protein and explain why