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Concept explainers
(a)
Interpretation:
The fragments obtained from the cleavage of given peptide chain by trypsin, cyanogen bromide and chymotrypsin should be given.
Concept introduction:
Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).
Endopeptidases cleave peptide bonds that are not at the end.
Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine and lysine.
Chymotrypsin is an endopeptidase, which cleave the C-side peptide bond of amino acids that contain
Cyanogen bromide cleaves the C-terminal peptide of Methionine in a peptide chain.
(b)
Interpretation:
The numbers of primary structure if the amino acids contained in each fragment are known has to be determined.
Concept introduction:
The number of primary structures in a polypeptide is determined by checking the number of disulfide bridges connected with primary structures.
Disulfide bridges are formed between thiol groups of cysteine.
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Chapter 17 Solutions
Essential Organic Chemistry Study Guide & Solution Manual, Books a la Carte Edition
- Nonearrow_forwardNonearrow_forwardWhat spectral features allow you to differentiate the product from the starting material? Use four separate paragraphs for each set of comparisons. You should have one paragraph each devoted to MS, HNMR, CNMR and IR. 2) For MS, the differing masses of molecular ions are a popular starting point. Including a unique fragmentation is important, too. 3) For HNMR, CNMR and IR state the peaks that are different and what makes them different (usually the presence or absence of certain groups). See if you can find two differences (in each set of IR, HNMR and CNMR spectra) due to the presence or absence of a functional group. Include peak locations. Alternatively, you can state a shift of a peak due to a change near a given functional group. Including peak locations for shifted peaks, as well as what these peaks are due to. Ideally, your focus should be on not just identifying the differences but explaining them in terms of functional group changes.arrow_forward
- Nonearrow_forwardNonearrow_forwardIn the solid state, oxalic acid occurs as a dihydrate with the formula H2C2O4 C+2H2O. Use this formula to calculate the formula weight of oxalic acid. Use the calculated formula weight and the number of moles (0.00504mol) of oxalic acid in each titrated unknown sample recorded in Table 6.4 to calculate the number of grams of pure oxalic acid dihydrate contained in each titrated unknown sample.arrow_forward
- 1. Consider a pair of elements with 2p and 4p valence orbitals (e.g., N and Se). Draw their (2p and 4p AO's) radial probability plots, and sketch their angular profiles. Then, consider these orbitals from the two atoms forming a homonuclear л-bond. Which element would have a stronger bond, and why? (4 points)arrow_forwardWrite the reaction and show the mechanism of the reaction. Include the mechanism for formation of the NO2+ 2. Explain, using resonance structures, why the meta isomer is formed. Draw possible resonance structures for ortho, meta and para.arrow_forwardNonearrow_forward
- Introduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage LearningGeneral, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage Learning
- Organic And Biological ChemistryChemistryISBN:9781305081079Author:STOKER, H. Stephen (howard Stephen)Publisher:Cengage Learning,Organic ChemistryChemistryISBN:9781305580350Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. FootePublisher:Cengage Learning
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