Concept explainers
(a)
Interpretation:
Bonding responsible for the sheet formation in
Concept introduction:
Many amino acids are linked together through amide bonds to form a biologically large molecule known to be proteins.
Amine
Secondary structure of protein is the repeating structural patterns (
Hydrogen bonding is an electrostatic attraction between hydrogen and an electronegative atom.
(b)
Interpretation:
The atoms responsible for hydrogen bonding are to be identified.
Concept introduction:
Many amino acids are linked together through amide bonds to form a biologically large molecule known to be proteins.
Amino functional group is
Secondary structure of protein is the repeating structural patterns (
Hydrogen bonding is an electrostatic attraction between hydrogen and an electronegative atom.
Want to see the full answer?
Check out a sample textbook solutionChapter 18 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
- 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.)arrow_forwardDraw the following Lipids in: A) Condensed (detailed) Structure, B) its Block Diagram. C) Show/Indicate the type of linkages per structure (put an arrow). 5) Glycosphingolipid/Sphingoglycolipid (use sphingosine, stearic acid, and D-galactose);arrow_forwardDraw the following Lipids in: A) Condensed (detailed) Structure, B) its Block Diagram.C) Show/Indicate the type of linkages per structure (put an arrow). 4) Sphingolipid/Sphingophospholipid (use sphingosine, myristic acid, phosphate, and choline for amino alcohol);arrow_forward
- Draw the Fischer projections representing the L forms of the following amino acids at pH higher than their isoelectric point. a) cysteine b) alaninearrow_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_forward1)Ubiquitin is a small protein with a monoisotopic mass of 8560 Da. a) Electrospray ionization of this small protein typically results in major charge states of +8, +9, +10, +11, +12, and +13. Using this information, complete the table below, assuming the charges on each come from protonation. Report mass and m/z values to the ones place. b) Using the data you entered in the table, sketch an expected ESI-MS spectrum for ubiquitin. Label each peak with its charge state. What do you notice about the spacing of peaks along the x-axis. c)The figure shows an experimentally obtained electrospray mass spectrum for ubiquitin. Compare this spectrum to the spectrum you predicted. Are there any differences? If so, what might cause these differences?arrow_forward
- Explain how a protein is denatured by the following: (a) Heat(b) Strong acids (c) Organic solventsarrow_forward(iii) Draw a structural diagram of a hydrogen bond between β-D-glucose and the side chain of any polar residue in a protein. (iv) Name the type of bond that can occur between the axial hydrogens of glucose and the indole ring of tryptophan. Draw a structural diagram of this bond. (v) Comment on the polar / apolar nature of the bond in part (iv) and explain why this type of interaction is prevalent in protein-sugar complexes. Answer (iii) to (v) please.arrow_forward(a) Draw an example of a triglyceride molecule and name the functional group that links the glycerol backbone to the side-chains derived from fatty acids. (b) The structure of a neuraminidase inhibitor is shown in Figure Q6b. This compound renders the influenza virus unable to escape its host cell and so controls further infection. Using your knowledge of amino acids, draw possible binding interactions that all functional groups in the inhibitor (except C7-OH) could make with the neuraminidase enzyme. + H HN. H + Arg152 NH, HN 12 Arg156 OH NHCCH, Glu119 OH -0 но ÓH H+ N. HN HN Arg118 HN' 2 + HN Glu276 + H Arg292 NH, HN NH2 Arg371 Neuraminidase Inhibitor (Figure Q6b)arrow_forward
- Examine the structure shown below. A) What is the common name for this fatty acid? B) What is the IUPAC Name for this fatty acid? (Note: you can use the letter D to represent A in the name).arrow_forwardDetermine the sequence of the following 10-mer of ferritin using the data below. i. Complete acid hydrolysis of the 10-mer results in identification of 1A, 1D, 1E, 1F, 1H, 1K, 2L, 1T, 1Y ii. Digestion of the 10-mer with chymotrypsin results in 3 fragments containing (D, H, K, T), (F, L) and (A, E, L, Y) iii. Digestion of the 10-mer with V8 protease, which cuts on the C-side of acidic amino acids, results in three fragments containing (D, F, L, Y), (A, E, L) and (H, K, T) iv. Digestion with trypsin results in a fragment H-T and a fragment with all the other amino acids v. Treatment of the 10-mer with FDNB followed by complete acid hydrolysis results in the following two derivatives, DNP-1 and DNP-2 vi. Treatment of the 10-mer with a carboxypeptidase results in a free threoninearrow_forwardWhich of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON