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Concept explainers
(a)
Interpretation: The building blocks which represents the fatty acid residues in the given block diagram of sphingophospholipid have to be predicted.
Concept introduction: In sphingophospholipids, the platform molecule is sphingosine to which one fatty acid and one phosphate group are attached. An alcohol is attached to the phosphate group. There are two ester linkages and one amide linkage present in the structure of sphingophospholipids. There are two ester linkages and one amide linkage present in the structure of sphingophospholipids.
(b)
Interpretation: The building blocks which represents the phosphate residues in the given block diagram of sphingophospholipid have to be predicted.
Concept introduction: In sphingophospholipids, the platform molecule is sphingosine to which one fatty acid and one phosphate group are attached. An alcohol is attached to the phosphate group. There are two ester linkages and one amide linkage present in the structure of sphingophospholipids. There are two ester linkages and one amide linkage present in the structure of sphingophospholipids.
(c)
Interpretation: The linkages which which represents the amide linkages in the given block diagram of sphingophospholipid have to be predicted.
Concept introduction: In sphingophospholipids, the platform molecule is sphingosine to which one fatty acid and one phosphate group are attached. An alcohol is attached to the phosphate group. There are two ester linkages and one amide linkage present in the structure of sphingophospholipids. There are two ester linkages and one amide linkage present in the structure of sphingophospholipids.
(d)
Interpretation: The linkages which involve a sphingosine residue in the given block diagram of sphingophospholipid have to be predicted.
Concept introduction: In sphingophospholipids, the platform molecule is sphingosine to which one fatty acid and one phosphate group are attached. An alcohol is attached to the phosphate group. There are two ester linkages and one amide linkage present in the structure of sphingophospholipids. There are two ester linkages and one amide linkage present in the structure of sphingophospholipids.
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Chapter 19 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- Classify the fatty acid with the following structural formula in the ways indicated.a. What is the type designation (SFA, MUFA, or PUFA) for this fatty acid? b. On the basis of carbon chain length and degree of unsaturation, what is the numerical shorthand designation for this fatty acid?c. To which “omega” family of fatty acids does this fatty acid belong? d. What is the “delta” designation for the carbon chain double-bond location for this fatty acid?arrow_forwardImagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. In the table below are four possibilities for what R, and R, might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ R₂ threonine cysteine glutamine arginine cysteine tyrosine phenylalanine glutamate specific interaction? Oyes no yes O no O yes O no Oyes O no name of specific interaction 0 0 0 0 Xarrow_forwardConsider the following situation; Fresh pineapple contains the enzyme bromelain that hydrolyzes peptide bonds in proteins. a. The directions in making a gelatin (protein) dessert say not to add fresh pineapple. However, canned pineapple where pineapple is heated to high temperatures can be added. Why? b. Fresh pineapple is used in a marinade to tenderize tough meat. Why? c. What structural level of a protein does the bromelain enzyme destroy?arrow_forward
- Draw the following sugars using Haworth projections:a. b-d-galactopyranose b. a-d-tagatopyranose c. a-l-glucopyranosearrow_forwardThe following are structural diagrams of a selection of newly discovered amino acids. OH -の-CHs NH HO C-OH NH, AN-CH CH2 CH2 OH Ho NH, C=0 a) Select 1 amino acid. Redraw it. Label the alpha carbon and circle/highlight the entire backbone of the amino acid. b) The amino acids are part of a channel protein embedded in the cell membrane. Choose 2 amino acids (from above) that you would expect to find within the interior/middle of the cell membrane. Draw the formation of the dipeptide using the 2 amino acids you selected. Identify the other products formed in the reaction.arrow_forwardWhich of the following is TRUE? Select one: a. The disulfide bridges formed by oxidation of the sulfhydryl groups on cysteine stabilizes protein tertiary structure. b. The disulfide bridges formed by oxidation of the sulfhydryl groups on cysteine destabilizes protein tertiary structure. c. The disulfide bridges formed by reduction of the sulfhydryl groups on cysteine stabilizes protein tertiary structure. d. The disulfide bridges formed by reduction of the sulfhydryl groups on cysteine destabilizes protein tertiary structure. Clear my choicearrow_forward
- At neutral pH, which of the following amino acids has a net positive charge, which has a net negative charge, and which is neutral? (Hint: Draw the various charged forms of each amino acid before deciding.)(a) Aspartic acid (b) Histidine (c) Valinearrow_forwardA schematic diagram of the helical structure of cytochrome b562 is reproduced below. Thisprotein belongs to the family of -proteins that have a four-helix bundle. Number the helices 1 – 4according to their N C direction. Indicate relative orientations of the macrodipoles of helices 1 – 4adjacent to the diagram of cytochrome b562. Remember that according to the definition of a dipolethat the arrow points towards the positive end.arrow_forwardhow does the protein environment surrounding an amino acid chain affect its chemical properties?Consider the carboxyl group on an asparate side chain in the following environments in a protein. Rank in order these environments from the highest to the lowest proportion of carboxyl groups in the -COO- form.that is in terms of pKas. 1. an aspartate side chain on the surface of protein with no other ionizable groups nearby. 2. an aspartate side chain buried in a hydrophobic pocket on the surface of a protein 3. an asparate chain in a hydrophobic pocket adjacent to a glutamte side chain 4. an asparate side chain in a hydrophobic porket adjacent to a lysine side chain.arrow_forward
- Draw a phosphorylated tyrosine molecule at physiological pH. Assume that the phosphate group is deprotonated and has a charge of -2. Would the carboxylic acid group of the phosphorylated tyrosine have a lower or higher pKa than that of unmodified tyrosine? Explain.arrow_forwardVitamin D3, the most abundant of the D vitamins, is synthesized from 7- dehydrocholesterol, a compound found in milk and fatty fish such as salmon and mackerel. When the skin is exposed to sunlight, a photochemical electrocyclic ring opening forms provitamin D3, which is then converted to vitamin D3 by a sigmatropic rearrangement. Draw the structure of provitamin D3.arrow_forwardAn oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.arrow_forward
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