Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
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Question
Chapter 2, Problem 32P
Interpretation Introduction
Interpretation:
The conformation of Pro-X peptide bonds needs to be compared with that of X-Pro peptide bonds.
Concept introduction:
Amino acids are compounds containing amino as well as acidic group. The general molecular structure of an amino acid is as follows:
Here, R is different group for different amino acids. If there is more than one amino group present in an amino acid, they are considered as basic amino acids and if there is more than one carboxylic group then they are considered as acidic amino acids.
Two or more amino acids combine to form di- or polypeptide chains. Here, peptide bond is the amide bond formed between the two amino acids.
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Students have asked these similar questions
the resonance stabilization of the amide linkage has profound
effects on protein structure. Which of the following are the direct effect(s) of this on
protein structure?
Select all that apply
All six atoms around the bond (including the Co) lie on the same plane
There is no free rotation about the peptide bond.
The bond between the carbon and the nitrogen in the peptide bond keeps
"flickering" between being a single bond and a double bond.
The peptide bond is polar.
The nitrogen in the peptide bond cannot accept a hydrogen bond.
Regarding the last answer choice, how come both alpha helices and beta sheets aren't denatured when the heat breaks peptide bonds? If heat were to break peptide bonds, wouldn't that affect the primary structure which inevitably affects the more complicated structures?
Be as detailed as you can possibly be.
Chapter 2 Solutions
Biochemistry
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34P
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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
- What would the net charge be of a polypeptide with the sequence M-D-R-N-Q-K-R-W at pH 8? hint ionizable groups include N-terminus (pKa = 9.0), D (pKa = 3.9), R (pKa = 12.5), K (pКa %3D 10.5) O +2 O-1 O +1arrow_forwardThe different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bondsarrow_forward1 onlyarrow_forward
- What is the charge of this peptide at pH 1.5?arrow_forwardWhich of the following is true of the molecule below? nucleotide 5' 3′ H₂C H₂C TNHNA O. HN CNH…NG NH O NH O HNU NH O CNHNG OHN nucleoside CH₂ CH₂ a purine pairs with a pyrimidine base the bases are held together by covalent bonds a nucleoside is made of the same components as a nucleotide The bases make up the backbone on the sides of the moleculearrow_forwardShow anabolism of two molecules of serine. Be sure to clearly identify each molecule and bond/linkage involved. Hand-draw the diagramarrow_forward
- How do covalent bonds differ from hydrogen bonds? Define base complementarity (refer to implementation of double helix) and describe why G-C bonding is stronger than A-T bonding (why is it important?)arrow_forwardWhat would the net charge be of a polypeptide with the sequence M-D-R-N-Q-K at pH 8? hint ionizable groups include N-terminus (pKa = 9.0), D (pKa = 3.9), R (pKa = 12.5), K (pKa = %3D %3D %3D %3D 10.5) O +2 O+1 O-1 00arrow_forward6. b. Draw a box around the disulfide bridge in oxytocin, if present, or write "none". 7. Mark each peptide bond in oxytocin by making the corresponding line in the structure thicker or marking it with a different color. The first one is shown for you as an example (in dark orange). 8. Number the central carbon of each amino acid in oxytocin by pointing a small arrow to it or by circling the corresponding vertex in the image. Numbers 1 and 2 indicate the central carbons of the first and second amino acids of oxytocin, and are shown for you as an example. 9. Fill out the following table, listing amino acids that make up oxytocin in order, from the N terminus to the C terminus, characterizing each amino acid by the properties of its R group (side chains), and briefly indicating the reasoning for the characterization. You may consult amino acid groupings by category in the slides (or the textbook, p.49), but you must explain the reasoning for each in your own words. CO 1 AA# Abbre- Full…arrow_forward
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