Which type of amino acid would be found on the outside of a portion of a protein embedded in the membrane (up close to the fatty acid tails)? Select one: O a. a special amino acid like glycine or proline Ob. a polar amino acid like serine c. a hydrophobic amino acid like valine Od. a charged amino acid like lysine O e. any of the above, with no preference Clear my choice

Which type of amino acid would be found on the outside of a portion of a protein embedded in the membrane (up close to the fatty acid tails)? Select one: O a. a special amino acid like glycine or proline Ob. a polar amino acid like serine c. a hydrophobic amino acid like valine Od. a charged amino acid like lysine O e. any of the above, with no preference Clear my choice

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Which of the following is an example of protein denaturation? * A. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone. B. Several amino acids are joined together together via peptide bonds. C. A protein binds with with a substrate, lowering the activation energy of reaction. D. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be left with only its primary structure. E. Results to unfolding, partial or incomplete disorganization of the protein's secondary and tertiary structure.
Which of the following types of molecular interactions play a role in protein folding? Select all that apply. A.)Hydrophobic interactions B.)Van der Waals attraction C.)Hydrogen bonds D.)Covalent bonds
Which of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic 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 statements are correct about the molten globular state of protein folding (select all that appy)? A. May be short-lived or long-lived intermediate in protein folding B. Contains substantial levels of secondary structure C. Has loose packing of hydrophobic core D. Larger radius of gyration than dentaured state E. Is a more compact state than the native confomation
Refer to the figure below. Replacing lysine with another amino acid in the protein may alter the shape and function of the protein. Replacing lysine with which type(s) of amino acid(s) would lead to the least amount of change in the tertiary structure of this protein? Explain your answer.
Which of the following statements are correct about the role of chaperones in protein folding (select all that appy)? A. Chaperones accelerate the rate of protein folding B. Presence of chaperones contradicts dogma that structure of protein is only determined by amino acid sequence C. Chapreone promotion of native folding is an ATP-dependent process D. Chaperones work by stabilizing hydrophobic patches on proteins E. A cell line with the GroEL and GroES deleted would accumulate more unfolded protein
Of the following amino acids, which 3 are most likely to be found on surface of a single protein. a) Arg b) Trp c) Cys d) Phe e) Leu f) Lys
Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?
Which of the following types of molecular interactions play a role in protein folding? Select all that apply. A. Covalent bonds B. Hydrogen bonds C. Van der Waals attraction D. Hydrophobic interactions
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
Which of the following, if any, is correct about protein folding? a)2° structure formation is primarily entropic, 3° structure formation is primarily entropic b)2° structure formation is primarily entropic, 3° structure formation is primarily enthalpic c)2° structure formation is primarily enthalpic, 3° structure formation is primarily entropic d)2° structure formation is primarily enthalpic, 3° structure formation is primarily enthalpic e)None of the above