Organic Chemistry - Standalone book
10th Edition
ISBN: 9780073511214
Author: Francis A Carey Dr., Robert M. Giuliano
Publisher: McGraw-Hill Education
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Chapter 26.17, Problem 25P
Interpretation Introduction
Interpretation:
The pattern of the methyl group orientation in the
Concept Introduction:
A
The geometry of the peptide bond is planar, with the two alpha carbons in anti conformation.
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Chapter 26 Solutions
Organic Chemistry - Standalone book
Ch. 26.1 - Prob. 1PCh. 26.2 - Prob. 2PCh. 26.2 - Prob. 3PCh. 26.3 - Prob. 4PCh. 26.3 - Prob. 5PCh. 26.4 - Prob. 6PCh. 26.4 - Prob. 7PCh. 26.4 - Prob. 8PCh. 26.5 - Prob. 9PCh. 26.6 - Prob. 10P
Ch. 26.6 - Prob. 11PCh. 26.6 - Prob. 12PCh. 26.7 - Prob. 13PCh. 26.7 - Prob. 14PCh. 26.7 - Prob. 15PCh. 26.7 - Prob. 16PCh. 26.7 - Prob. 17PCh. 26.9 - Prob. 18PCh. 26.10 - Digestion of the tetrapeptide of Problem 26.18...Ch. 26.12 - Prob. 20PCh. 26.12 - Prob. 21PCh. 26.15 - Prob. 22PCh. 26.15 - Prob. 23PCh. 26.16 - Prob. 24PCh. 26.17 - Prob. 25PCh. 26.18 - Prob. 26PCh. 26 - Prob. 27PCh. 26 - Prob. 28PCh. 26 - Prob. 29PCh. 26 - Prob. 30PCh. 26 - Prob. 31PCh. 26 - Prob. 32PCh. 26 - Prob. 33PCh. 26 - Prob. 34PCh. 26 - Prob. 35PCh. 26 - Prob. 36PCh. 26 - Prob. 37PCh. 26 - Prob. 38PCh. 26 - Prob. 39PCh. 26 - Prob. 40PCh. 26 - If you synthesized the tripeptide Leu-Phe-Ser from...Ch. 26 - Prob. 42PCh. 26 - Prob. 43PCh. 26 - Prob. 44PCh. 26 - Prob. 45DSPCh. 26 - Prob. 46DSPCh. 26 - Prob. 47DSPCh. 26 - Prob. 48DSPCh. 26 - Prob. 49DSPCh. 26 - Prob. 50DSP
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- 22-64 If both cysteine residues on the B chain of insulin were changed to alanine residues, how would it affect the quaternary structure of insulin?arrow_forward22-42 (a) How many atoms of the peptide bond lie in the same plane? (b) Which atoms are they?arrow_forwardHow many of the -amino acids shown in Table 26-1 contain aromatic rings? How many contain sulfur? How many contain alcohols? How many contain hydrocarbon side chains?arrow_forward
- How do I identify which amino acid is more soluble in water in alanine vs. leucine structures?arrow_forwardIf you were to design a small peptide with a large net negative charge at physiological pH, which amino acid residues should predominate?arrow_forwardClassify the following characteristics as a type of 3D protein structure. Primary, Secondary, Tertiary or Quaternary. a. Singular unit held together by cross-links b. Singular sequence of amino acids С. Combination of two or more protein unitsarrow_forward
- Which one did I miss? What did I do wrong? Select the true statements about protein secondary structure. Peptide bonds stabilize secondary structure. The B-pleated sheet is held together by hydrogen bonds between adjacent segments. In a B-pleated sheet, the side chains extend above and below the sheet. In an a-helix, the side chains are located inside the helix. The secondary level of protein structure refers to the spatial arrangements of short segments of the protein.arrow_forwardWhat type of chemical bond stabilizes the protein secondary structure, such as the alpha helix shown below. O Hydrogen bond O Salt bridge O Hydrophobic interaction O Disulfide bridge U=O....H -Z U=O... HIZ 010 HIN ····HINI CIO....H C=O... Harrow_forwardMatch the pair of amino acids in first column with the type of side- chain interaction the pair is capable of. leucine and valine 1. Hydrophobic interaction 2. Disulfide bond threonine and serine 3. Metal ion coordination lysine and arginine 4. Hydrogen bond alanine and threonine 5. Salt bridge histidine and aspartic acid 6. None >arrow_forward
- 8. The following proteins represent a wide range of molecular weights and isoelectric points. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) • Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at pH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated ammonium sulfate? Explain your answer. 5 83°F Cloudyarrow_forward5) Identify each of the following observations about protein or 4' structure A. Amino acids 14-38 in the sequence are arranged in structure as being aspects of the 1', 2', 3', a-helix pattern. B. When the protein was enzymatically broken apart, one of the fragments was found to be Ala-Lys. C. The entire molecule is globular 1.3 times as long in Leu-Tyr-Gly- one dimension as its diameter. D. Detergent was added to a water solution of the protein. The molecular weight study before the addition indicated a single protein with a molecular weight of 150,000. After the addition, two proteins were present with molecular weights 25,000 and 50,000.arrow_forward3. Draw the tripeptide Alanine-Cysteine-Serine (R1 = CH3, R2 = CH2SH, R3 = CH2OH) under the following pH conditions and list the net charge on the protein. A. pH= 1 Net charge? B. pH=7 Net charge? C. pH=12 Net charge?arrow_forward
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