Biological Science (6th Edition)
6th Edition
ISBN: 9780321976499
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Emily Taylor, Greg Podgorski, Jeff Carmichael
Publisher: PEARSON
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Chapter 3, Problem 13PIAT
Summary Introduction
To determine:
The frequency of proline to appear in peptide, if it were made up of a completely random assortment of the 20 most common amino acids
Given:
One of the peptides that can be recovered after gluten digestion is 33 residues long; 13 of the 33 residues are proline.
Introduction:
Gluten proteins are rich in amino acid proline, so they do not break down easily during digestion in small intestine, resulting in short and long peptides. These peptides can be broken down further and absorbed through the intestine and further can be utilized by the body.
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On paper draw a dipeptide, clearly showing the peptide bond joining the two amino acids together. If the two amino acids are valine and threonine, predict the overall charge of the dipeptide at pH 7. Do not forget to consider the amino (N-terminal) and carboxy (C-terminal) of the dipeptide, as well as the R groups.
Select one:
a. +2
b. -2
c. 0
d. -1
e. +1
Biochemistry,based on the example,need help to
1)hand draw the dipeptides that contains Glutamic acid and Proline.
2)hand draw the tetra peptides that contains Glycine , Alanine,Glutamic acid and Proline.
Biochemistry : How to calculate percentages of arginine 's side chain have positively charge at PH=7
Chapter 3 Solutions
Biological Science (6th Edition)
Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - 2. What type of bond is directly involved in the...Ch. 3 - What type of information is used to direct...Ch. 3 - 4. What is an active site?
a. the location in an...Ch. 3 - Prob. 5TYUCh. 3 - Prob. 6TYUCh. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 8TYUCh. 3 - Prob. 9TYPSSCh. 3 - 10. Make a concept map (see BioSkills 12) that...
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- a. The graph to the right displays the degree of helicity that was measured for a peptide as nine additional amino acids were sequentially added to the initial amino acid. Describe the reasons that the helicity curve takes the shape that it does as amino acids are added on to the small peptide.arrow_forwardCalculate the Rf values for each of the amino acids and enter your data in the table.Based on your calculations, what is the identity of the Unknown amino acid? Rank the amino acids from most hydrophilic to most hydrophobicarrow_forwardConsider the peptide EAHIVR. Write out the sequence of the peptide from N to C in three letter code. Draw the complete structure of the peptide including all peptide bonds and side chains at pH 8.0. Calculate the pI of this peptide. Calculate the net charge of this peptide at pH 2, pH 7, and pH 11.arrow_forward
- Calculate the approximate molecular weight of a protein composed of 587 amino acid residues in a single polypeptide chain. approximate weight: in kDaarrow_forwardExplain the Rf value obtained on the basis of the structure of amino acids use. Explain in 1-3 sentence only.arrow_forwardChemistry Why does glutamate (when spatially positioned nearby) raise the pka of a histidine, but not alanine or arginine ?arrow_forward
- Biochemistry : How to calculate percentages of arginine have positively charge at PH=7arrow_forwardChemistry explain how the change is chemical character that occurs with the missense mutation will influence the tertiary or quaternary structure of the protein (FGFR3). How will the change in shape cause LOF or GOF. be specific! amino acid in missense mutation= S249C serine: polar uncharged, phosphorylated cysteine: nonpolar or polar, disulfide bondarrow_forwardNeed help The β chains of HbA and HbS were treated with trypsin, and the sequence of the N-terminal tryptic peptides are as given below. Do these peptides separate from each other in an electric field if the pH is 7.0? Explain in detail the reasoning behind your answer and include your calculations for the charge of each peptide in your answer. HbA: Val-His-Leu-Thr-Pro-Glu-Glu-Lys HbS: Val-His-Leu-Thrarrow_forward
- Briefly explain why the size and weight of a protein are not directly proportional to the number of amino acid residues it contains. (think about the properties of different amino acids)arrow_forwardmake a diet recall from the situation for gordon's functional patternarrow_forwardA peptide was analyzed with the following results. What is the primary structure of the peptide? State what each experimental result reveals about the structure and indicate your logic. a) Amino acid analysis: R, C (2 equivalents), G, I, H, M, Y, Vb) After one round of Edman degradation, a mixture of glycine and isoleucine were detected. c) Treatment with beta-mercaptoethanol yielded two peptides, a 4-mer and a 5-mer.arrow_forward
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