Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 2, Problem 2P
Draw two different possible hydrogen-bonding interactions between two molecules of formamide (HCONH2). Clearly label the hydrogen-bond donor and acceptor atoms. Which of these two possible hydrogen-bonding interactions is more likely to occur? (Hint: Consider resonance structures for formamide.)
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Draw a schematic of the chemical structure of the Leu-Tyr-Met-Lys tetrapeptide, with the
correct ionization at neutral pH (pH 7). Also, give an estimate the pl of this tetrapeptide (you
are given that the pKa of any acidic R group is 4, the pKa of any basic R group is 11.5, and the
pKa of the α-COOH is 2, and the a-NH3 is 9.5). Provide rationale!
Determine the net charge on the following pentapeptide "Lys-Ala-His-Asp-Ser" at:
a. pH 1.0
b. pH 10.1
1) (10 points) Draw a schematic of the chemical structure of the Leu-Tyr-Met-Lys tetrapeptide,
with the correct ionization at neutral pH (pH 7). Also, give an estimate the pl of this
tetrapeptide (you are given that the pKa of any acidic R group is 4, the pKa of any basic R
group is 11.5, and the pKa of the a-COOH is 2, and the a-NH3 is 9.5). Provide rationale!
Chapter 2 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 2 - Suppose a chloride ion and a sodium ion are...Ch. 2 - Draw two different possible hydrogen-bonding...Ch. 2 - Prob. 3PCh. 2 - 4. What is the pH of each of the following...Ch. 2 - Prob. 5PCh. 2 - The weak acid HA is 2% ionized (dissociated) in a...Ch. 2 - 7. Calculate the pH values and draw the titration...Ch. 2 - What is the pH of the following buffer mixtures?...Ch. 2 - a. Suppose you wanted to make a buffer of exactly...Ch. 2 - Prob. 10P
Ch. 2 - You need to make a buffer whose pH is 7.0, and you...Ch. 2 - Describe the preparation of 2.00 L of 100 glycine...Ch. 2 - Carbon dioxide is dissolved in blood (pH 7.4) to...Ch. 2 - What is the molecular basis for the observation...Ch. 2 - The anno acid arginine ionizes according to the...Ch. 2 - It is possible to make a buffer that functions...Ch. 2 - A student is carrying out a biological preparation...Ch. 2 - Histidine is an amino acid with three titratable...Ch. 2 - Prob. 19PCh. 2 - A biochemical reaction takes place in a 1.00 ml...Ch. 2 - Is RNA-binding enzyme RNase A more likely to have...Ch. 2 - Consider a protein in which a negatively charged...Ch. 2 - Prob. 23PCh. 2 - Prob. 24P
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- With the aid of a simple generic diagram: i) IDENTIFY and EXPLAIN how the type(s) of chemical bonding stabilizes a SECONDARY structure that is present in 3GRS(Glutathione Reductase)??? https://www.rcsb.org/ ii) Describe why position 58 (Cysteine ) in 3GRS is important ??? and outline the Effects of the mutation from Cysteine 58 (Cys) to Glycine(GLY) will have on the 3D structure?? Effect of the mutation from Cysteine 58 (Cys) to Glycine (Gly )will have on the function of 3GRS?? I am stuck! please help only correct answers pls!arrow_forwardWith the aid of the simple generic diagram, identify and explain how the type of chemical bonding stabilizes a secondary structure present in 3GRS (glutathione reductase).arrow_forwardConsider the following fatty acid attached below. a) What is the number convention for this fatty acid above, including the location of the double bond from the α carbon end? Remember to use the Δ (delta) in your answer for the double bond location b) What is the ω (omega) numbering of the double bond for the fatty acid above? c) What is the product after two hypothetical additional rounds of synthesis for the fatty acid? Remember that synthesis adds 2 carbons at a time to the carboxylic end.arrow_forward
- (a) A decapeptide has the following amino acid composition: Alaz, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides: Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly. Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine om the experimental data, deduce the primary structure of the decapeptide.arrow_forwardA NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrazine Acid Hydrolysis (6 N HCI) at 110°C Nonapeptide (2) Arg, Gln, (2) Tyr, Gly, Ser, Thr, and Met 2,4-dinitrofluorobenzene DNP-Thr Gin and modified free amino acids Peptide 1 (Arg, Thr, Ser) Cleavage with Trypsin, then chromatography Peptide 2 (Gly, Tyr, Arg) Met Tripeptide Cyanogen bromide Dipeptide Peptide 3 (Arg, Ser, Tyr, Thr) Cleavage with Chymotrypsin, then chromatography Amino acid Peptide 4 (Gly, Arg, Tyr)arrow_forwardA NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrazine Acid Hydrolysis (6 N HCI) at 110 "C Nonapeptide (2) Arg, Gln, (2) Tyr, Gly, Ser, Thr, and Met 2,4-dinitrofluorobenzene DNP-Thr Gin and modified free Peptide 1 (Arg, Thr, Ser) amino acids Cleavage with Trypsin, then chromatography Peptide 2 (Gly, Tyr, Arg) Met Tripeptide Cyanogen bromide Dipeptide Peptide 3 (Arg, Ser, Tyr, Thr) Cleavage with Chymotrypsin, then chromatography Amino acid Peptide 4 (Gly, Arg, Tyr)arrow_forward
- Draw the structure of the peptide DTLH, showing the backbone and sidechainatoms in the ionization states favored at pH = 7.0.(a) Draw a water molecule making a hydrogen bond to a side-chain H-bonddonor.(b) Draw a water molecule making a hydrogen bond to a main-chain H-bond acceptor. (c) Using the values of pKas given in as shown, calculate the pI for DTLH.arrow_forwardDraw the Ala-Ser-Leu-Asp polypeptide (perspective formula) showing the fully extended backbone geometry (all angles +/- 180°). Include correct stereochemistry for L-amino acids. Label all bond rotations representing the angles at each residuearrow_forwardThe key reaction steps in the Edman degradation of polypeptides, which removes the N-terminal amino acid in the form of a "phenylthiohydantoin" (PTH-amino acid), are shown below. What is the expected outcome if the N-terminal amino acid is proline (Pro)? (The structure of proline is provided below for your reference.) NH-C00 NH CO0 phenyl isothiocyanate PITC NH CO0 NH CO0 peptide without the thiszolinone original Nterminal amino acid HE a PTH-amino acid Proline: HN HN. O Edman's reagent will not react with an N-terminal proline.arrow_forward
- Draw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in acqueous solution at pH=10.3. (Relevant pKa values are: 2.2,4.3,6.0,9.8 and 10.1)arrow_forwardFor the following amino acids select the INCORRECT alternative: (a) At pH = 4 all migrate towards the cathode except Asp. (b) At pH = 10 all migrate towards the anode. (c) The pI of phenylalanine (Phe) will be about 5.5. (d) The pl of aspartic acid (Asp) will be about 2.8. (e) At pH = 7 the amino acids Arg and Lys migrate towards the cathode and the rest to the anode.arrow_forwardThe following amino acid is dissolved in solution at pH 7.4. HC H' + CH CH₂ H/ H+ HC a. Which amino acid is this? (all lower case) N- H CH CH₂ b. What is the pKa of its ionizable side chain? (Use the value from the textbook.) c. What is the ratio of the uncharged to the charged form at pH 7.4? (write answer as number with one decimal place, ex 2.5 or 0.2 or 50.0 with an implicit "to 1")arrow_forward
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