
Introduction To General, Organic, And Biochemistry
12th Edition
ISBN: 9781337571357
Author: Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher: Cengage Learning
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Chapter 21, Problem 80P
Interpretation Introduction
Interpretation:
The number of ways can you link the two amino acids lysine and valine in a dipeptide should be determined. The peptide bonds that can be found in proteins should be identified.
Concept Introduction:
A peptide bond present in proteins is formed by the reaction of the
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Chapter 21 Solutions
Introduction To General, Organic, And Biochemistry
Ch. 21.1 - Prob. 21.1QCCh. 21.2 - Prob. 21.2QCCh. 21.3 - What is the overall charge (+,0, or ) for the...Ch. 21.4 - Problem 22-1 Show how to form the dipeptide...Ch. 21.5 - Prob. 21.5QCCh. 21.7 - Prob. 21.6QCCh. 21.8 - Prob. 21.7QCCh. 21.8 - Prob. 21.8QCCh. 21.10 - Prob. 21.9QCCh. 21 - 22-5 What are the functions of (a) ovalbumin and...
Ch. 21 - 22-6 The members of which class of proteins are...Ch. 21 - 22-7 What is the function of an immunoglobulin?Ch. 21 - Prob. 4PCh. 21 - 22-9 What is the difference in structure between...Ch. 21 - 22-10 Classify the following amino acids as...Ch. 21 - 22-11 Which amino acid has the highest percentage...Ch. 21 - Prob. 8PCh. 21 - Prob. 9PCh. 21 - Prob. 10PCh. 21 - Prob. 11PCh. 21 - Prob. 12PCh. 21 - 22-17 What are the similarities and differences in...Ch. 21 - 22-18 Draw the structures of L- and D-valine.Ch. 21 - Prob. 15PCh. 21 - 22-20 Show how alanine, in solution at its...Ch. 21 - 22-21 Explain why an amino acid cannot exist in an...Ch. 21 - 22-22 Draw the structure of valine at pH 1 and at...Ch. 21 - Prob. 19PCh. 21 - 22-24 Draw the most predominant form of histidine...Ch. 21 - 22-25 Draw the most predominant form of lysine at...Ch. 21 - Prob. 22PCh. 21 - 22-27 Show by chemical equations how alanine and...Ch. 21 - 22-28 A tetrapeptide is abbreviated as DPKH. Which...Ch. 21 - 22-29 Draw the structure of a tripeptide made of...Ch. 21 - 22-30 (a) Use the three-letter abbreviations to...Ch. 21 - 22-31 A polypeptide chain is made of alternating...Ch. 21 - Prob. 28PCh. 21 - 22-33 Which of the three functional groups on...Ch. 21 - Prob. 30PCh. 21 - 22-35 Why is histidine considered a basic amino...Ch. 21 - Prob. 32PCh. 21 - Prob. 33PCh. 21 - 22-38 Why does proline not absorb light at 280 nm?Ch. 21 - Prob. 35PCh. 21 - Prob. 36PCh. 21 - Prob. 37PCh. 21 - 22-42 (a) How many atoms of the peptide bond lie...Ch. 21 - 22-43 (a) Draw the structural formula of the...Ch. 21 - 22-44 How can a protein act as a buffer?Ch. 21 - 22-45 Proteins are least soluble at their...Ch. 21 - 22-46 How many different tripeptides can be made...Ch. 21 - 22-47 How many different tetrapeptides can be made...Ch. 21 - 22-48 How many amino acid residues in the A chain...Ch. 21 - 22-49 Based on your knowledge of the chemical...Ch. 21 - Prob. 46PCh. 21 - 22-59 What is the effect of salt bridges on the...Ch. 21 - Prob. 48PCh. 21 - 22-61 Polyglutamic acid (a polypeptide chain made...Ch. 21 - 22-62 Distinguish between intermolecular and...Ch. 21 - 22-63 Identify the primary, secondary, and...Ch. 21 - 22-64 If both cysteine residues on the B chain of...Ch. 21 - 22-65 (a) What is the difference in the quaternary...Ch. 21 - Prob. 54PCh. 21 - Prob. 55PCh. 21 - Prob. 56PCh. 21 - Prob. 57PCh. 21 - Prob. 58PCh. 21 - 22-71 Which amino acid side chain is most...Ch. 21 - 22-72 What does the reducing agent do in...Ch. 21 - 22-73 Silver nitrate is sometimes put into the...Ch. 21 - 22-74 Why do nurses and physicians use 70% alcohol...Ch. 21 - Prob. 63PCh. 21 - (Chemical Connections 21B ) AGE products become...Ch. 21 - Prob. 65PCh. 21 - Prob. 66PCh. 21 - Prob. 67PCh. 21 - Prob. 68PCh. 21 - Prob. 69PCh. 21 - 22-84 How many different dipeptides can be made...Ch. 21 - 22-85 Denaturation is usually associated with...Ch. 21 - Prob. 72PCh. 21 - Prob. 73PCh. 21 - Prob. 74PCh. 21 - 22-89 What kind of noncovalent interaction occurs...Ch. 21 - Prob. 76PCh. 21 - 22-91 Which amino acid does not rotate the plane...Ch. 21 - 22-92 Write the expected products of the acid...Ch. 21 - 22-93 What charges are on aspartic acid at pH 2.0?Ch. 21 - Prob. 80PCh. 21 - Prob. 81PCh. 21 - Prob. 82PCh. 21 - 22-97 Gelatin is derived from collagen by...Ch. 21 - Prob. 84PCh. 21 - Prob. 85PCh. 21 - Prob. 86PCh. 21 - 22-101 Using what you know about protein...Ch. 21 - 22-104 Why is collagen not a very good source of...Ch. 21 - Prob. 89P
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- 5. Propose a Synthesis for the molecule below. You may use any starting materials containing 6 carbons or less (reagents that aren't incorporated into the final molecule such as PhзP do not count towards this total, and the starting material can have whatever non-carbon functional groups you want), and any of the reactions you have learned so far in organic chemistry I, II, and III. Your final answer should show each step separately, with intermediates and conditions clearly drawn. H3C CH3arrow_forwardState the name and condensed formula of isooxazole obtained by reacting acetylacetone and hydroxylamine.arrow_forwardState the name and condensed formula of the isothiazole obtained by reacting acetylacetone and thiosemicarbazide.arrow_forward
- Provide the semi-developed formula of isooxazole obtained by reacting acetylacetone and hydroxylamine.arrow_forwardGiven a 1,3-dicarbonyl compound (R1-CO-CH2-CO-R2), indicate the formula of the compound obtaineda) if I add hydroxylamine (NH2OH) to give an isooxazole.b) if I add thiosemicarbazide (NH2-CO-NH-NH2) to give an isothiazole.arrow_forwardAn orange laser has a wavelength of 610 nm. What is the energy of this light?arrow_forward
- The molar absorptivity of a protein in water at 280 nm can be estimated within ~5-10% from its content of the amino acids tyrosine and tryptophan and from the number of disulfide linkages (R-S-S-R) between cysteine residues: Ε280 nm (M-1 cm-1) ≈ 5500 nTrp + 1490 nTyr + 125 nS-S where nTrp is the number of tryptophans, nTyr is the number of tyrosines, and nS-S is the number of disulfide linkages. The protein human serum transferrin has 678 amino acids including 8 tryptophans, 26 tyrosines, and 19 disulfide linkages. The molecular mass of the most dominant for is 79550. Predict the molar absorptivity of transferrin. Predict the absorbance of a solution that’s 1.000 g/L transferrin in a 1.000-cm-pathlength cuvet. Estimate the g/L of a transferrin solution with an absorbance of 1.50 at 280 nm.arrow_forwardIn GC, what order will the following molecules elute from the column? CH3OCH3, CH3CH2OH, C3H8, C4H10arrow_forwardBeer’s Law is A = εbc, where A is absorbance, ε is the molar absorptivity (which is specific to the compound and wavelength in the measurement), and c is concentration. The absorbance of a 2.31 × 10-5 M solution of a compound is 0.822 at a wavelength of 266 nm in a 1.00-cm cell. Calculate the molar absorptivity at 266 nm.arrow_forward
- How to calculate % of unknown solution using line of best fit y=0.1227x + 0.0292 (y=2.244)arrow_forwardGiven a 1,3-dicarbonyl compound, state the (condensed) formula of the compound obtaineda) if I add hydroxylamine (NH2OH) to give an isooxazole.b) if I add thiosemicarbazide (NH2-CO-NH-NH2) to give an isothiazole.arrow_forwardComplete the following acid-base reactions and predict the direction of equilibrium for each. Justify your prediction by citing pK values for the acid and conjugate acid in each equilibrium. (a) (b) NHs (c) O₂N NH NH OH H₁PO₁arrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY