Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
Chapter 3, Problem 22P
Interpretation Introduction
(a)
Interpretation:
The pH-dependent conformational transition in the poly-L-lysine should be determined.
Concept introduction:
Nuclear Magnetic Resonance (NMR) spectroscopy is an
Interpretation Introduction
(b)
Interpretation:
The identification of the pH dependence of the helix-coil transition of poly-L-glutamate should be determined.
Concept introduction:
Nuclear Magnetic Resonance (NMR) spectroscopy is an analytical chemistry method used in quality control and research for identifying the content and purity of a sample along with its molecular structure.
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i. A schematic structure of the subunit of hemerythrin (an oxygen-binding
protein from invertebrate animals) is shown to the right.
(a) It has been found that in some of the a-helical regions of hemerythrin,
about every third or fourth amino acid residue is a hydrophobic one.
Suggest a structural reason for this finding.
(b) What would be the effect of a mutation that placed a proline residue at
point A in the structure?
. Apamine is a small protein toxin present in the venom of the honeybee. It
has the sequence
CNCKAPETALCARRCQQH
(a) If apamine does not react with iodoacetate (see Tools of Biochemistry
5B), then how many disulfide bonds are present?
(b) If trypsin cleavage gave two peptides, then where is(are) the S-S
bond(s)?
The melting curve for the polyribonucleotide poly(A) is shown below. (a) Explain why absorbance increases with increasing temperature. (b) Why does the shape of the curve differ from the one shown in Fig. ?
Chapter 3 Solutions
Biochemistry
Ch. 3 - Prob. 1PCh. 3 - Prob. 2PCh. 3 - Prob. 3PCh. 3 - Prob. 4PCh. 3 - Prob. 5PCh. 3 - Prob. 6PCh. 3 - Prob. 7PCh. 3 - Prob. 8PCh. 3 - Prob. 9PCh. 3 - Prob. 10P
Ch. 3 - Prob. 11PCh. 3 - Prob. 12PCh. 3 - Prob. 13PCh. 3 - Prob. 14PCh. 3 - Prob. 15PCh. 3 - Prob. 16PCh. 3 - Prob. 17PCh. 3 - Prob. 18PCh. 3 - Prob. 19PCh. 3 - Prob. 20PCh. 3 - Prob. 21PCh. 3 - Prob. 22PCh. 3 - Prob. 23PCh. 3 - Prob. 24PCh. 3 - Prob. 25PCh. 3 - Prob. 26PCh. 3 - Prob. 27PCh. 3 - Prob. 28PCh. 3 - Prob. 29PCh. 3 - Prob. 30PCh. 3 - Prob. 31P
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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
- A. Write the structure of the following peptide at pH 5.0 and calculate its net charge at this pH. Asp-His-Tyr-Arg-Lys-Leu-Thr-Gln. Based on the pKa value of the ionizable groups. B. A polypeptide consisting only of L-glutamate residues (poly-L-glutamate) may have a random coil or helical structure depending on pH. Explain this behavior by indicating at what pH values the helical structure will be favored.arrow_forwardShape and dimension. (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α-helical coiled coil. Estimate the length of the molecule. (b) Suppose that a 40-residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?arrow_forward. Draw Haworth projections for the following: (a) CHO in a-furanose form. Name the sugar. H-C-OH | HO-C-H H-C-OH CH,OH (b) The L isomer of (a) (c) a-D-GlcNAc (d) a-D-Fructofuranosearrow_forward
- . Consider a small protein containing 101 amino acid residues. The protein will have 200 bonds about which rotation can occur. Assume that three orientations are possible about each of these bonds. (a) Based on these assumptions, about how many random-coil conforma- tions will be possible for this protein? (b) The estimate obtained in (a) is surely too large. Give one reason why.arrow_forwardConsider a protein with two surface-exposed histidine residues: HisA is a “typical” histidine residue with a pKa = 6.2 HisB is involved in a stabilizing interaction (His-NH+ ..... -O2C-Glu) with a neighboring glutamic acid residue. For HisB, the Gibbs free energy of deprotonation at pH = 7.0 and T = 293K is ΔG'o = +15 kj mol-1. If you had a solution, at pH = 7.0 and T = 293K, containing this protein: a) What fraction of HisA residues are protonated? b) What fraction of HisB residues are protonated? c) What is the pKa of HisB?arrow_forward. Assume that some protein molecule, in its folded native state, has one favored conformation. But, when it is denatured, it becomes a "random coil," with many possible conformations. (a) What must be the sign of AS for the change: native → denatured? (b) How will the contribution of AS for native → denatured affect the favorability of the process? What apparent requirement does this impose on AH if proteins are to be stable structures?arrow_forward
- -. A schematic structure of the subunit of hemerythrin (an oxygen- binding protein from invertebrate animals) is shown below. (a) It has been found that in some of the a-helical regions of hemerythrin, about every third or fourth amino acid residue is a hydrophobic one. Suggest a structural reason for this finding. (b) What would be the effect of a mutation that placed a proline residue at point A in the structure? A Fearrow_forwardComponents of Complex Biomolecules Figure 1-10 (Lehninger's Biochemistry book) shows the major components of complex biomolecules. For each of the two important biomolecules below (shown in their ionized forms at physiological pH), identify the constituents. And show H-bonding with water. (a) Guanosine triphosphate (GTP), an energy-rich nucleotide that serves as a precursor to RNA: N- NH -CH2 0- NH2 H H H H. ОН ОН (b) Phosphatidylcholine, a component of many membranes: CH3 O- CH3*N-CH2-CH2-0-P-0–CH2 нн CH3 НС —О—С—(CH), —С—С— (CH), — СHз CH,–0-C-(CH,)14–CH3arrow_forwardA synthetic polypeptid made up of L-glutamic acid residues is in a random coil configuration at pH 7.0 but changes to alpha helical when the pH is lowered to 2.0. Explain this pH-dependent conformational transition.arrow_forward
- Suppose that there is a protein consisting of two polypeptide chains with the given sequences in the picture. What will be the expected result if a biochemist does an end-group analysis to identify the N and C terminal residues of the protein? Explain why.arrow_forward. Give two reasons to explain why a proline residue in the middle of an ahelix is predicted to be destabilizing to the helical structurearrow_forwarda. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).arrow_forward
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