Where is hydrogen bonding observed in proteins? Between one part of the protein backbone and another part of the protein backbone Between R groups Between the protein backbone and an R group All of the above
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- Describe the four levels of protein structure. How do a proteins side groups influence its interactions with other substances? What happens when a protein is denatured?ch one of the following statements about protein structure is NOT correct? . Domains are discrete parts of a protein structure, usually associated with a particula function. true Beta-sheets are stabilised by hydrogen bonds between amino-hydrogens and carbonyl-oxygens from peptide bonds. no adjacent hydrogen bonding Proteins made from three polypeptide chains show quaternary structure. Yes Smaller protein domains come together to from supersecondary structures and moWhich 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.
- 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…Which 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 subunitsWhen 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 groups
- Which of the following levels of protein architecture is least likely affected by changes in pH? O Secondary Structure Quaternary Structure O Tertiary Structure O Primary StructureHydrogen bonds that form a helices and B-pleated sheets are the primary interaction in which level of protein structure? O secondary O quaternary O primary O tertiary(a) Are all proteins polymers? What is the basie unit of protein? Explain the formation of Zwitterion in a-amino acid. (b) Count the number of peptide bonds in the below structure. -R-N-C-R-N-C-R-N-C-R-N-C- wwww H H H H
- 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 interactionsGive the force of interaction involved in the protein folding of the protein structure A and C: COO CH,C-N-H• • •0- Pleated sheet structure A H C Helical structure CH3 CH3 - CH3 -CHCH,CH, CH- CH, CH3 (CH,),NH, -0-CCH,- C=0..•HN CH, CH, CH,CH CH,CH CH, CH, CH OH 0=C -CH,-S,S-CH,- H,Ñ Structure A: H-bonding: Structure C: Van der Waals O Structure A: Covalent interaction; Structure C: dipole-dipole interaction O Structure A: Salt bridge: Structure C: H-bonding Structure A: Hydrophobic interaction; Structure C: ionic interaction 00000 BMatch the following levels of protein structure with their description two or more polypeptide chains > > twisting and folding to form a 3-dimensional structure, dependent on the locations of the charged groups and polar groups within the amino acid chain, sometimes covalent bonds form between sulfur atoms (called disulfide bonds) alpha helix and beta- pleated sheets formed by the arrangement of hydrogen bonds between amino acids, many other shapes are possible amino acid sequence 1. quaternary 2. tertiary 3. primary 4. secondary