What causes a protein to fold? A. Chemical interactions between the specific R-groups of the protein chain B. Chemical interactions that draw certain nucleotides together C. Chemical attractions between amino groups and acid groups that form covalent bonds D. The protein folds into the shape that is most physically stable, depending upon the number of amino acids in the chain

What causes a protein to fold? A. Chemical interactions between the specific R-groups of the protein chain B. Chemical interactions that draw certain nucleotides together C. Chemical attractions between amino groups and acid groups that form covalent bonds D. The protein folds into the shape that is most physically stable, depending upon the number of amino acids in the chain

Human Biology (MindTap Course List)

11th Edition

ISBN:9781305112100

Author:Cecie Starr, Beverly McMillan

Publisher:Cecie Starr, Beverly McMillan

Chapter2: Chemistry Of Life

Section: Chapter Questions

Problem 7RQ: Describe the four levels of protein structure. How do a proteins side groups influence its...

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Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
How does the coplanar nature of the peptide bond impact the overall structure of a protein? O a. It facilitates the stacking of aromatic side chains. O b. It promotes the flexibility of the protein backbone. Oc. It restricts the formation of secondary structures. Od. It allows for the easy formation of disulfide bonds. It constrains the rotation around the peptide bond, influencing protein folding.
What is one of the determining factors in the three-dimensional structure of a protein? A.The location of alpha sheets and beta propellersB.The presence of another proteinC.The location of hydrophobic and hydrophilic amino acidsD.The presence of nucleic acids such as DNA
Which of the following statements about protein structure is CORRECT O a. Fibrous proteins can have rigid quaternary structure O b. The stability of the quaternary structure in proteins is mainly a result of covalent bonds among the subunits O c. The denaturation of proteins always leads to irreversible loss of secondary and tertiary structure d. The information required for the correct folding of a protein is contained in the specific sequence of amino acids along the polypeptide chain O e. The formation of a disulfide bond in a protein requires that the two participating cysteine residues be adjacent to each other in the primary sequence of the protein
Which statement(s) correctly describe(s) protein structures?A. All hydrophobic residues are buried when protein structures and protein aggregatesB. Charged and polar amino acid residues are seldom buried in the protein interior C. Lysine is found only in the protein interiorD. Glycine is rarely found in proteins due to its destabilizing effect A,B,C A,C B B,C,D
Which of the following events would have the strongest influence on the overall three-dimensional structure of a protein? Select one: a. Valines angle away from surrounding water molecules as the protein folds b. Two polypeptide strands, running in opposite directions, form hydrogen bonds with each other Oc. Another protein sticks to its outside d. The amine and carboxylic ends of the protein chain are left unreacted Oe. Three glycines are chained together Clear my choice Previous page esc ! 1 ← 2 3 W 3 E 38 $ 4 R 5 T 80 MacBook Pro A 6 Y & 7 U 8 I 9 4 1 O 0 P TO + ( W Next pa
What life uses proteins for? (functions of proteins) Describe protein structures. Describe the alpha helix and the beta sheet structure of proteins. Which structure is the most important in the function of a protein? Describe what can affect the protein structure. Why the structure of a protein is important?
Understand that some amino acids are nonpolar, polar/uncharged, charged. Explain how this is related to the 4 levels of protein structure.
A protein has a mutation of a glycine to a lysine. Which best predicts the impact of this mutation on the overall protein structure and function? H.N, *NH3 Glycine Lysine O A small hydrophobic amino acid has been replaced with a large hydrophilic amino acid, and this may change folding O A small hydrophilic amino acid has been replaced with a large hydrophobic amino acid, and this may change folding O These residues are similar in chemical properties, and there will be little impact on folding O This mutation may disrupt hydrogen bonds, which would disrupt the tertiary structure
What is the general characteristic of protein domains? A. All protein domains exhibit both a and B structures B. Protein domains constitute supersecondary structures that have specific biological functions in proteins. C. Most protein domains can be hydrolyzed from parent polypeptide chains while retaining functions and/or structures that are conserved. D. Protein domains constitute the structural block from which the protein is built E. Protein domains contain motifs that are the binding sites for prosthetic groups such as heme, or the iron-sulfur clusters.
Which of the following is the most fundamental determinant of the conformation of a protein? O a. The location of cysteine amino acids within the protein O b. The pH of the solution O c. Hydrogen bonding within the molecule O d. The primary structure of the protein O e. The quaternary structure
Give at least 10 functions of protein and describe each function. Cite an example for each function if there are any.