6. The tertiary structure of proteins is typified by the: There are 20 different

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6. The tertiary structure of proteins is typified by the: There are 20 different amino acids in the proteins that make up the tissues of living organisms. The primary difference between these amino acids is in their: association of several polypeptide chains by weak bonds. 1. a. b. order in which amino acids are joined in a a. R or variable groups. b. number of potassium groups. c. number of phosphate groups d. number of carbonyl groups. e. number of asymmetric carbons peptide chain bonding of two amino acids to form a dipeptide. folding of a peptide chain to form an alpha helix. three-dimensional shape of an individual polypeptide chain c. d. e· The bonding of two amino acid molecules to form a larger molecule requires 7. Which of the following is responsible for the alpha-helical structure of proteins? 2. a b. c. d. e. hydrophobic interactions nonpolar covalent bonds ionic interactions hydrogen bonds polar covalent bonds a. b. c. d· e. The release of a water molecule. The release of a carbon dioxide molecule. The addition of a nitrogen atom. The addition of a water molecule. The release of a nitrous oxide molecule. The amino acids of the protein keratin are arranged predominantly in an a helix. This secondary structure is stabilized by 8. 3. At which level of protein structure are peptide bonds most a primary b. secondary c. tertiary d. quaternary e. globular a. Covalent bonds. b. Peptide bonds. c. Ionic bonds. d. Polar bonds. e. Hydrogen bonds. What is the term used for a protein molecule that assists in the proper folding of other proteins? 4. Some proteins are important biological buffers because: 9. a. they react with water to produce carbon dioxide, which neutralizes acids they contain weakly acidic and weakly basic groups. they are able to absorb great amounts of carbon dioxide during condensation reactions. they produce carbonic acid upon hydrolysis. All of the above. a. tertiary protein b. c. enzyme protein d. renaturing protein e. denaturing protein c. d. e. When a protein is denatured, why does it lose its functionality? a. The protein's pH changes, causing it to lose its 10. All of the following types of chemical bonds are responsible for maintaining the tertiary structure of this polypeptide except: 5. functionality Denaturation destroys the primary structure of the protein, and the protein breaks down to b. a. ionic bonds. b. hydrogen bonds. c. hydrophobic interactions. d. disulfide bonds. c. peptide bonds. Denaturation breaks the weak bonds, such as hydrogen bonds and van der Waals interactions that hold the protein in its three-dimensional shape. Without the proper shape, the protein cannot function. Denaturation breaks the covalent bonds that hold the protein in its three-dimensional shape. c. d. Without the proper shape, the protein cannot function. Different amino acids are substituted into the sequence, so the protein's properties changs e.

Explanation / Answer

1. Correct answer is "A" - R or Variable Group

Explanation : The Primary difference between these amino acids is R group, Based on R group it can be differentiated.

2. Correct answer is "D" - Hydrogen Bonds

Explanation : Alpha helical structure is secondary structure of protiens, Hydrogen bonds are responsible for alpha helical structure of protiens as it is back bone.

3. Correct answer is "A" - Primary Structure

Explanation : Peptide bonds are formed in primary Structure, basing on these Secondary structure are formed

4. Correct answer is "B" - They contain weekly acidic and weekly basic groups

Explanation : Some protiens are important biological buffers beacause they contain weekly acidic and weekly basic groups

5. Correct answer is "E" - Peptide Bonds

Explanation- Ionic bonds, Hydrogen bonds,disuphide bonds, hydrophobic interactions all these responsible for maintaining teritiary structure

6. Correct answer is "E" - Three dimensional shape of an individual polypeptide chain.

Explanation : The teritiary structure of protiens is typfied by the three dimensional shape of an individual polypeptide chain. structure of every protien has three dimensional shape

7. Correct answer is " A' - The release of water molecule

Explanation : During peptide bond formation in protiens release of water molecules happens

8. Correct answer is " E' - Hydrogen bonding

Explanation : Hydrogen bonding is main responsible for secondary structure in protiens stabilised by this bonding

9. Correct answer is - "B" - Chaperonin

Explanation : Chaperonin are main responsible for protien folding

10. Correct answer is - "D" - Denaturation breaks down covalent bond that holds protein in its three dimensional shape. with out proper shape the protien cannot function

Explanation : Function of protiens depends on shape

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