The figure above shows some of the more common modifications, such as phosphorylation (1), acetylation or methylation (2), adding sugars or lipids (3,4), or adding another polypeptide (5). There are many other possibilities as well.Find and label each of these on the diagram. How might these modifications affect the protein?

The figure above shows some of the more common modifications, such as phosphorylation (1), acetylation or methylation (2), adding sugars or lipids (3,4), or adding another polypeptide (5). There are many other possibilities as well.Find and label each of these on the diagram. How might these modifications affect the protein?

Biology Today and Tomorrow without Physiology (MindTap Course List)

5th Edition

ISBN:9781305117396

Author:Cecie Starr, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Christine Evers, Lisa Starr

Chapter7: Gene Expression And Control

Section: Chapter Questions

Problem 2CT

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1. Use the info of this molecule as well as the attached addendum to demonstrate the flow of genetic information to protein sequence as described by the so-called “Central Dogma” . Clearly indicate the direction of your polynucleotide strands and peptide/protein. ATG GCA TGC AAT AGC TCA TGC 2. What would happen to the amino acid sequence if the underlined nucleotide (C) would change to an A?
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1) what is the net charge of the amino acid leucine of it is on the C-terminus end and why? 2) if the amino acid was changed to lysine on the c-terminus end explain why and what the net charge would be?.
1.a.If this molecule was the side chain of an amino acid, in a protein, what tertiary structure stabilizers could be present? b.Make a key and use color to highlight what part of you structure can be stabilized in each manner?
Refer to the figure below. Replacing lysine with another amino acid in the protein may alter the shape and function of the protein. Replacing lysine with which type(s) of amino acid(s) would lead to the least amount of change in the tertiary structure of this protein? Explain.
4. Amino acids are linked together by peptide bonds to form polypeptides. (a) Draw the structure of a tripeptide (b) draw an asterisks (*) directly beside all alpha carbons and draw a square around all peptide bonds (c) Use arrows to identify and label the N-terminus and C-terminus (d) Draw a circle around the R group of each amino acid residue in the tripeptide and classify each R group as polar, non polar, acidic, or basic (e) Using the abbreviated names of the amino acids, provide the primary structure of the tripeptide you have drawn.
1 What is the dominant biochemical activity or molecular interaction that your protein is predicted to carry out? Which sites on the protein contribute to the process directly? Which sites contribute indirectly? protein = amyloid-beta precursor
6a) Transcribe the following DNA sequence into codons. TACGCGACATTACATGAATCGTTTGGAGATTAGCCCTATTTCTCTAAGAACACGACTb) Excise(cut out) codons numbered 5, 6, and 7. Leave the remaining codons. c) Now translate the sequence . d) Explain how many amino acids are now in your polypeptide? e) What would happen to your polypeptide if either of your cysteine amino acids near the start or end of thepolypeptide were translated incorrectly. f) Based on your final polypeptide can you make the original DNA strand by doing reverse translation andtranscription? g) Explain if your polypeptide similar to your template strand or the complementary strand?
D. Draw the structure of Histidine and Imidazole. Why do you think we use Imidazole to elute the protein? Why do we use a 6X His tag?
1. Explain why is it necessary for a protein to adopt specific tertiary and quaternary arrangements. 2.Explain the role of hydrogen bonding and disulfide bonds between R groups. 3. Explain the similarities and differences between rna and dna.
A protein with which of the following sequences may be more prone to undergo farnesylation? (a) Trp-Ala-Ala-Cys (b) Ser-Gly-Gly-Glu (c) Ser-Ala-Ala-Trp (d) Cys-Leu-Leu-Ser
1. A certain polypeptide was treated with trypsin and yielded the following Fragments: Leu-Glu Gly-Tyr-Asn-Arg Gln-Ala-Phe-Val-Lys The same polypeptide was treated with chymotrypsin and yielded the following fragments: Gln-Ala-Phe Asn-Arg-Leu-Glu Val-Lys-Gly-Tyr What is the amino acid sequence of this polypeptide? Instructions Make use of the table below to determine the sequence of the mystery protein.