
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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Briefly describe whey amino acids with hydrophobic side chains (R-groups) tend to cluster on the inside of folded polypeptides.
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- Consider an amino acid sequence: D1-G2-M3-E4-C5-A5-F7-H8-R9-I10-A11-H12-T13-Y14-G15-F16-P17-E18-A19-A20-M21-C22-K23-W24-E25-A26-Q27-P28 The β-turn structure is likely found at (Write down the residue number). A possible disulfide bond is formed between the residues and . The total number of basic residues are The addition of chymotrypsin will result in blank peptide fragment(s). The addition of trypsin will result in blank peptide fragment(s). The addition of CNBr will result in blank peptide fragment(s).arrow_forwardWhat are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved. The molecule considered is a protein: pancreatic amylase.arrow_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
- Within a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the following amino acids always has a negatively charged carboxyl group? the first amino acid in the primary structure histidine lysine arginine the last amino acid in the primary structurearrow_forwardGlutamine is an amino acid that has -CH₂-CH2-CO-NH₂ as its R group. The R group of the amino acid isoleucine is -CH2-CH-(CH3)2. If these amino acids were in a globular protein in aqueous solution, where would they most likely be? O Both glutamine and isoleucine would be in the interior and on the exterior of the globular protein. O Glutamine would be in the interior, and isoleucine would be on the exterior of the globular protein. O There isn't enough information O Both glutamine and isoleucine would be on the exterior of the globular protein. O Isoleucine would be in the interior, and glutamine would be on the exterior of the globular protein.arrow_forward2) Consider the following disaccharide which was formed from the breakdown of a polysaccharide found in plant material. ОН Glycosidic linkage: H H OH H H НО H H. OH H. ОН OH H НО H ОН a. Label the glycosidic linkage above in the following format: a/B(# → #) b. Would you expect this disaccharide to have been formed from amylose or amylopectin? c. Describe at least two chemical tests that would give insight into the structure of this disaccharide, assuming you've isolated it and wanted to elucidate the structure from scratch. Include detail on not only the tests you would use but what results you would expect to get given the structure above. Assume you can analyze the structure of any monosaccharide you get from your chemical tests.arrow_forward
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