An alpha-helical structure within a protein is stabilized mostly by O hydrophobic interactions. O hydrogen bonding between the backbone groups. O disulfide linkages. hydrogen boding between the amino acid side chains.
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"An alpha-helical structure within a protein is stabilized mostly by"
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- Which one of the following statements about the structure of proteins is incorrect? O Disulfide bonds provide strong intrachain interactions. Hydrogen bonding stabilizes the a-helix proteins. Nonpolar groups tend to face the outside of a protein in an aqueous solution. lonized amino acid side chains can form salt bridges within a protein. O Heat can disrupt tertiary structure.Which of the following factors do not stabilize the 3-D structure of a folded protein? O Disulfide bonds O Van der Waals interactions O Hydrogen bonds O Electrostatic interactions O Hydrophobic bonds Metal-ion protein interactionsWhich of the which of the following forces are involved in maintaining the primary structure of a protein? covalent bonds hydrogen bonds ionic interactions hydrophobic interactions
- When a protein folds into a quaternary structure the outside amino acids are exposed to the aqueous (water rich) environment. These amino acid R likely have what chemical properties? O The amino acid R groups are polar and hydrophilic The amino acid R groups are non-polar and hydrophobic O The amino acid R groups have hydrocarbon functional groups O The amino acid R groups have unreactive functional groupsProteins occurring in the b-pleated sheet structure Multiple Choice are relatively inelastic. produce structurally weak materials never occur in nature. contain no peptide bonds. are not involved in hydrogen bonds.The secondary structure of a protein is determined by the association with other proteins. O hydrogen bonding between amino acids. the amino group of the amino acid. the carboxyl group of the amino acid.
- What is the major difference between tertiary and quaternary protein structure? The sequence of amino acids involved. The involvement of R (radical) groups. The number of polypeptides involved.Encircle ALL PEPTIDE BONDS in the givenWhich of the following constitutes the primary structure of a protein? O the folding of a polypeptide chain the polypeptide chains stacked on top of each other O the linear sequence of amino acids in a polypeptide chain several polypeptide subunits
- Proteins with alpha-helical forms exhibit this property: O strength. O elasticity. O heat stability. O rigidity. O hydrophobicity.Protein structure is directly related to function. Which of the following statements is true regarding this concept ? Polypeptide backbone -CH2 – CH, – CH2- CH2- NH3 0-c- CH - CH2 lonic bond Hydrogen ! bond C- NH2 Disulfide linkage CH CH2 HạC CH3 CH3 H3C CH -CH2 Hydrophobic interactions A. The primary structure consists of the DNA sequence. The secondary and tertiary structures are dependent on interactions between the DNA and RNA polymerase. Mutations resulting in changes one or more bases has the potential to destroy the structure, and therefore the function, of the protein. B. The primary structure consists of the amino acid sequence. The secondary and tertiary structures are dependent on interactions between the amino acid side chains. Mutations resulting in changes one or more amino acids has the potential to destroy the structure, and therefore the function, of the protein. C. The primary structure consists of the DNA sequence. The secondary structure consists of the amino acid…Hydrophobic interactions associated with protein tertiary structure involves: Acidic and basic amino acid side chains All of the above Nonpolar amino acid side chains Hydrogen bonding between polar amino acid side chains