33. Which of the following amino acid structures would be found usually on the surfaces of protein? A. I and IV B. I only C. II and III D. II only E. None of the above 34. Amino acid found in the surface is A. Hydrophilic; Hydrophobic B. Hydrophobic; Nonpolar C. Hydrophilic; Polar D. Hydrophobic; Hydrophilic E. None of the above while amino acid found in the interior is 35. Which of the 20 essential amino acids is unique because of its chemical property that readily dimerizes in the presen of mild oxidizing agents? A. Glycine B. Lysine C. Methionine D. Leucine E. None of the above

33. Which of the following amino acid structures would be found usually on the surfaces of protein? A. I and IV B. I only C. II and III D. II only E. None of the above 34. Amino acid found in the surface is A. Hydrophilic; Hydrophobic B. Hydrophobic; Nonpolar C. Hydrophilic; Polar D. Hydrophobic; Hydrophilic E. None of the above while amino acid found in the interior is 35. Which of the 20 essential amino acids is unique because of its chemical property that readily dimerizes in the presen of mild oxidizing agents? A. Glycine B. Lysine C. Methionine D. Leucine E. None of the above

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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This image shows the tertiary structure of a protein segment. Tertiary structure results from different interactions, or forces, between groups. Move the example of each force to the appropriate description on the protein. Then, identify the major force controlling tertiary structure. (Need help) It says I'm wrong.
A protein has a clearly defined hydrophobic core; however there is the residue glutamine within the hydrophobic core. How is this residue most likely stabilized (aka ‘made happy’) within this hydrophobic core? a. Hydrophobic interactions b. Interactions with a metal ion c. Hydrogen bonds d. Ionic interactions e. Electrostatic interactions
Describe the amino acid illustrated above (at pH = 7.0).A. it is a polar, negatively-charged amino acidB. it is a non-polar, negatively-charged amino acidC. it is a polar, positively-charged amino acidD. it is a non-polar, positively-charged amino acidE. it is a non-polar, uncharged amino acid
Which of the following is true regarding proteins A. Absorbance of proteins is directly proportional to the molecular weights B.Proteins react with biuret reagent because of their side chains C. two out of the twenty amino acids can absorb at 280nm D. In proteins the average weight per amino acid residue always varies
Discuss using your own words and illustrations the organisation of a protein, from its linear amino acid sequence, to its final three–dimensional configuration, which may include one or more polypeptides. Include what types of bonds help to stabilise each structural level, from primary through quaternary structure.
A. What type of bond is ( the two mark wtih questions mark) B. What special amino acid side chain is involved in forming these bond C. Does this bond form unde reduction or oxidizing D. Is this bond seen more in cytoplsmic proteins or in extravellular protein
Protein β-sheets are most likely to be found in: a either the interior or exterior of proteins, with no preference for one or the other. b the exterior of proteins, exposed to the aqueous environment. c the interior of proteins, away from the aqueous environment.