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Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 2, Problem 5P
Interpretation Introduction
Interpretation:
The following amino acids have R groups that have hydrogen-bonding potentials needs to be identified.
Ala, Gly, Ser, Phe, Glu, Tyr, Met, and Thr
Concept introduction:
Amino acids are organic compounds containing amino as well as
Here, R group is different for different amino acids. This group can be acidic, basic or neutral.
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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.
Which of the following amino acids have R groups that have hydrogen- bonding potential? Ala, Gly, Ser, Phe, Glu, Tyr, Ile, and Thr
Shown below is the structure of a polypeptide with the pK, values of its acidic hydrogens.
pK =
= 10.1
H
OH pK, = 9.2
H.
pKa = 2.1 H.
N-H pK, = 6.0
pKa = 3.9
1. How many peptide bonds are present in one molecule of the polypeptide?
[ Select ]
II. Over what pH range would this molecule predominantly exist in a state that has a net charge of zero?
[ Select ]
ZI
Chapter 2 Solutions
Biochemistry (Looseleaf)
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. 34PCh. 2 - Prob. 35PCh. 2 - Prob. 36PCh. 2 - Prob. 37P
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- What tertiary interaction would be expected between the following amino acids HN- OH HN- CH- OH CH-CH, covalent bond electrostatic attraction O hydrogen bonding O hydrophobic O no tertiary interaction expectedarrow_forwardThe The interconversion between the two forms of guanine base shown below is called form of guanine is the one shown on the left and the from is shown on the right. H. N. H. N. H. N. H. но tautomeric shift; amino; imino deamination; amino; deaminated alkylation; alkylated; hydroxylated tautomeric shift; keto; enol oxidation; reduced; oxidizedarrow_forwardA polypeptide with a net positive charge at physiologic pH (~7.4) most likely contains amino acids with R groups of what type? Aliphatic R groups Basic R groups O Aromatic R groups O Acidic R groupsarrow_forward
- Which of the following shows the reaction by which valine and leucine form a peptide bond H. H. H O -COO H2N-C-C-NH- C- C-OH + HO CH2 CH,SH ČH3 А. C. CH(CH)2 H. HN-C-C-NH-C- C-OH H,N-CH-C- + H,O HC-C-H CH2 CH2 H CH3 CH H,C-C-H CH(CH3)2 CH В. D.arrow_forwardChoose Two. The Ramachandran plot indicates: B H Ca ||||||| Ⓒ. The C1 I A. Combined preference about both H しょしい O conformation preference for a C1-C² and c²_N bonde Existence of a peptide in an a-helical conformation Or P sheeted The prefered conformation about Can bond. The prefered conformation about C1-C² bond The prefesed conformation about peptide bond.arrow_forwardProteins are quite stable. The lifetime of a peptide bond in aqueous solution is nearly 1000 years. However, the free energy of hydrolysis of proteins is negative and quite large. How can you account for the stability of the peptide bond in light of the fact that hydrolysis releases much energy?arrow_forward
- Chemistry Draw the stable form of the peptide Ser-Trp-Glu-Asp-Cys-Asn at pH 10.40. Be sure to explicitly label every N, O, S as well as H that is not attached to carbon in the main chain and indicate a rectangle to identify the six atoms that are coplanar with the peptide bond between residue 2 and 3 in the peptidearrow_forwardThe tertiary structure of a protein is maintained by interactions between the side chains of amino acid residues one such interaction is between cysteine residues, sketch a covalent bond link that can form between side chains of two cysteine residues. Only relevant atoms that can form the link need to be shownarrow_forwardDraw out the basic amino acid structure (not specific) What is a peptide bond?arrow_forward
- the overall, net ionic charge on this peptide at pH = 7 would be: Cys - Ala - Glu-Arg - Met - Serarrow_forwardA peptide bond... is a version of an ester bond is a version of an amide bond is the basis of protein secondary structure is formed by addition of waterarrow_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
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