4. Now returning to the topic of endogenous peptides, the sequence for a-endorphin is: YGGFMTSEKSQTPLVT a) Convert the one-letter code sequence for a-endorphin into the corresponding three-letter code sequence. For example, IKEA will be lle-Lys-Glu-Ala b) Which amino acid is at each terminus of a-endorphin? N-term: C-term c) Which amino acid in a-endorphin has a sidechain that is positively charged at pH 7.4? d) Which amino acid in a-endorphin has a sidechain that is negatively charged at pH 7.4? e) How many amino acids in a-endorphin contain a hydroxyl group?

4. Now returning to the topic of endogenous peptides, the sequence for a-endorphin is: YGGFMTSEKSQTPLVT a) Convert the one-letter code sequence for a-endorphin into the corresponding three-letter code sequence. For example, IKEA will be lle-Lys-Glu-Ala b) Which amino acid is at each terminus of a-endorphin? N-term: C-term c) Which amino acid in a-endorphin has a sidechain that is positively charged at pH 7.4? d) Which amino acid in a-endorphin has a sidechain that is negatively charged at pH 7.4? e) How many amino acids in a-endorphin contain a hydroxyl group?

Biology: The Unity and Diversity of Life (MindTap Course List)

15th Edition

ISBN:9781337408332

Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Chapter9: From Dna To Protein

Section: Chapter Questions

Problem 5SQ: The main function of a DNA molecule is to ________ . a. store heritable information b. carry a...

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7. Which of the following events does NOT take place in/on the RER? a. cleavage of the signal recognition peptide b. biosynthesis of core oligosaccharides for N-linked glycosylation c. Phosphorylation of mannose to give rise to mannose-6-phosphate. d. attachment of a core oligosaccharide to protein via asparagine residues e. cleavage of GTP by SRP receptor
1. What is the length in AA’s of the LilP protein? Assume fMet is NOT CLEAVED. 2. Write out the sequence of the polypeptide in AA: use the three letter notation, e.g. Met-Ser-Pro-
4. The strength of ligand-protein binding is a property of the binding site called --------------
6. Please describe the events that may result in a mature protein not having methionine asthe N-terminal amino acid.
1. Considering the following nucleotide sequence in an mRNA molecule: 5’ AUG UUA CGU AAU GCU GUC GAA UCU AUU UGC UUU ACA UAA 3' d) Write the amino acid sequence of the peptide synthesized from the given mRNA nucleotide sequence. e) Draw the structure of the pertide fragment made up of the first five (5) amino acids in the given polypeptide.
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?
2. A mixture of the following amino acids (glu, leu, val, arg, ser, phe) was obtained upon complete hydrolysis of a hexapeptide. a. Edman’s reagent releases leucine b. Hexapeptide with carboxypeptidase releases serine. c. Hexapeptide with trypsin forms a tripeptide A with leucine at the N terminal and tripeptide B with valine at the N terminal. d. Tripeptide A with carboxypeptidase releases arginine and a dipeptide with glutamic acid at C terminal. e. Tripeptide B with chymotrypsin form releases serine and another dipeptide. Give: 1. the amino acid sequence of tripeptide A and B. 2. the amino acid sequence in the above hexapeptide.
3. How does dimerization of a receptor tyrosine kinase promotes autophosphorylation of the intracellular domain of the receptor? How does the formation of a dimer helps the phosphorylation reaction?4. Describe where is the phosphate group added on a protein when it gets phosphorylated (what amino acid? what atom?). Then list all the ways that protein function may change after it gets phosphorylated PLEASE ANSWER BOTH
What is the difference between a peptide and a protein? 2. What type of bond is the peptide bond? Explain why the peptide bond is rigid. 3. The pentapeptide Gln-Tyr-Asn-Ala-Asp is present in human cerebrospinal fluid, and its concentration increases in demyelinating diseases. In these diseases, the myelin sheath of nerves is damaged and impairs the conduction of nerve signals. a. What is the N-terminal amino acid? b. What is the C-terminal amino acid? c. How many peptide bonds does this pentapeptide contain? From how many amino acids is this pentapeptide derived? d. Write the structure, the three-letter designation and the IUPAC name of this pentapeptide.
2. What is the minimum number of single nucleotide substitutions that would be necessary for each of the following amino acid replacements? a. Trp to His b. Met to His
4. Within a few months of hosting her podcast, Diamond learns that one of her listeners is concerned about mild depression and a loss in appetite. Diamond plans to invite a Registered Dietitian Nutritionist and Therapist to the podcast to discuss the importance of amino acids and serotonin as it relates to depression and restlessness. Which amino acid helps to build serotonin? a. arginine b. thyroxin c. proline d. tryptophan e. glutamine 5. Based on Diamond's weight, how much protein should she be consuming every day? a. about 25 g b. about 37 g c. about 44 g d. about 56 g e. about 62 g
A peptide containing 18 amino acid residues in its sequence was partially hydrolyzed and peptides A–D were detected in the resulting mixture. Draw the sequence of the original peptide.A Phe-Gly-AlaB Ser-Ser-Ser-Trp-Phe-Gly-AlaC Phe-Phe-Met-Ala-Ala-Pro-Trp-CysD Met-Ala-Ala-Pro-Trp-Cys-Leu-Ile-Leu-Ser-Ser