Biochemistry: Concepts and Connections
1st Edition
ISBN: 9780321839923
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Textbook Question
Chapter 5, Problem 2P
Draw the structure of the peptide DTLH, showing the backbone and side-chain atoms.
a. Draw a water molecule making a hydrogen bond to a side chain H-bond donor.
b. Draw a water molecule making a hydrogen bond to a main chain H-bond acceptor.
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One photo is the explanation and the other one is the question
a. Identify the type of mutation shown below.
b. How many amino acids are affected?
c. What type of impact will this mutation have on the functionality of the protein?
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Original DNA strand G
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Third letter
a. Identify the type of mutation shown below.
b. How many amino acids are affected?
c. What type of impact will this mutation have on the functionality of the protein?
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Chapter 5 Solutions
Biochemistry: Concepts and Connections
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Some alpha helices might be amphipathic. Where exactly in the protein structure would you find this type of helices. Explain how the position of amino acids in the sequence defines the structure of such helices. a. b.arrow_forwardIdentify which of the following pairs of amino acid residues can have hydrogen bonding between their side chains.a. Alanine and Glycineb. Leucine and Isoleucinec. Valine and Asparagined. Threonine and Tyrosine2. Draw a picture showing the details of the hydrogen bonding among the pairs in exercise 1arrow_forwarda. Identify the type of mutation shown below. b. How many amino acids are affected? c. What type of impact will this mutation have on the functionality of the protein?arrow_forward
- When answering the questions below, please use the ONE-LETTER CODE for the amino acid, with NO spaces and symbols between each letter.a. What is the C-terminal residue? b. What is the N-terminal residue? c. What is the sequence of Peptide 2? d. What is the sequence of Peptide 4? e. What is the overall amino acid sequence?arrow_forwardPropose one amino acid substitution that would disrupt the leucine zipper structure and explain whyarrow_forwardshow aarrow_forward
- Please give explanation of answer.arrow_forwardA biotechnology company focused on peptide therapeutics is investigating the properties of several peptides for a variety of applications. Their sequences are given below: Pep A: NGSLGAAGRG Pep B: KKALLAHALH Pep C: LVQAIFPTPS a. What is the net charge of each sequence at pH 7 (to the nearest 0.1 charge unit)? b. Which peptide sequence would be most likely to be part of an intrinsically ordered domain in a protein? Explain. c. Which peptide would likely be best suited as part of a pH-sensitive drug carrier that is designed to change its charge between neutral pH and endosomal pH (which is between 5 and 6)? Explain. d. Which peptide sequence would be most likely to be buried in the interior of a protein? Explain.arrow_forwardDescribe the catabolism of a the amino acid serine. Start with serine and end with ATP. Give the details of every step.arrow_forward
- Which of the following could be the DNA template for the following protein primary structure. Methionine - Alanine - Asparagine - Aspartic Acid - Phenylalanine - Glutamine - stop O a. 3' TACCGGTTACTGAAAGTTATT 5' O b. 3' AUGGCCAAUGACUUUCAAUAA 5' O c. 5' ATGGCCAATGACTTTCAATAA 3' O d. 5' TACATGTAACAAGACGCCAAT 3"arrow_forwardCan you help find the charge for the c terminal?arrow_forwardDraw the structures for nordihydrocapsaicin, capsaicin, and dihydrocapsaicin. How are they structurally related? a. How do their side chain structures differ in terms of carbon chain length and degree of unsaturation? b. What portion of the capsainoid molecular structure contributes the most to its hydrophobicity?arrow_forward
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