What is the general characteristic of protein domains?A. All protein domains exhibit both a and B structuresB. Protein domains constitute supersecondary structuresthat have specific biological functions in proteins.C. Most protein domains can be hydrolyzed from parentpolypeptide chains while retaining functions and/orstructures that are conserved.D. Protein domains constitute the structural block fromwhich the protein is builtE. Protein domains contain motifs that are the binding sitesfor prosthetic groups such as heme, or the iron-sulfurclusters.

Proteins are linear heteropolymers of twenty standard amino acids attached through the peptide…

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Why do some proteins contain D-amino acids? A. D-amino acids will determine the binding of the protein to its interacting partners. B. D-amino acids will determine whether the structure will be recognized and digested by naturally occurring enzymes C. D-amino acids determines the reactions the proteins will undergo. D. D-amino acids determines the solubility of the protein in aqueous solution. OE. A combination of D and L-amino acids is necessary for the proper folding of protein structures in aqueous solutions.
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.
For lipids, explain why the nonpolar tails have clustered together.
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
a. which amino acid can form a covalent bond with its side chain? b. which amino acid can contribute to protein tertiary and quarternary structure by forming a covalent bond?
The following diagram shows a short piece of a protein. Use the diagram to answer the following questions. A. What three amino acids are present in the segment? B. How many peptide bonds are present? C. Which amino acid is at the N terminus?
1. Is there more than one way to fold a protein, given the conflicting demands of the different "R" groups and the protein existing in a watery environment? 2. Explain what an R group is. 3. Compare the backbone of a polypeptide with that of a nucleic acid. 4. Proteins perform critical functions in all of our cells. Without proteins, life wouldn’t exist. Think of some specific proteins and describe what function they perform. 5. Explain the difference between secondary and tertiary protein structures.
Which of the following statements is/are TRUE for globular proteins? A. sensitive to changes in pH & heat B. regular amino acid sequence C. soluble in water D. structural role
Which of the following statements is incorrect? A.- the structure and charge of the proteins have direct effects on the rate of its migration through the gel matrix include b.- SDS is a type of a buffer with strong protein-denaturing effect and binds to the protein backbone at a constant molar ratio c.- SDS and polyacrylamide gel largely eliminates the influence of the structure and charge, and proteins are separated solely based on polypeptide chain length. d.When proteins are separated by electrophoresis through a gel matrix, smaller proteins appears at the lower portion of the gel
When a protein is denaturated, what happens to it?Describe two causes of denaturation.
Draw a sketch of a lipid bilayer, the structure that forms when a lipid such as phosphatidyl serine is dissolved in water.
1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric point of the amino acids are as follows; histidine 7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.

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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.