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…

Answered: What is the general characteristic of…

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter3: Biological Macromolecules

Section: Chapter Questions

Problem 2VCQ: Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble...

See similar textbooks

Similar questions

Protein Structure and Folding:a. Explain how changes in a protein’s amino acid sequence can change the way it behaves in water.b. Explain how changes in a protein’s amino acid sequence can change the way it interacts with othermolecules.c. Explain how changes in a protein’s amino acid sequence can change the way it forms secondary andtertiary structures when placed in water.
What are four levels of protein structure, and explain how a protein's shape determines its function? Explain denaturation.
a.Describe the bonds which hold a quaternary protein molecule together. b. Discuss the reasons why glycine and proline are not usually found in an alpha helix of proteins.
Can u explain How does the sequence of amino acids determine protein function? How does molecular shape influence protein function?
Characterize the four levels of protein structure and describe thepattern of folding.
Using examples, describe the four levels of protein structure.
A portion of a polypeptide chain contains the following sequence of amino acids: (-Met, -Leu, -Ala, -Cys, -Asp-) a.) Which amino acid can form a disulfide bond? b.) Which amino acids are likely to make the polypeptide more soluble in water? c.) Which amino acids are likely to make the polypeptide less soluble in water? d.) How does the primary structure of a protein affect its tertiary structure?
Which level of protein structure organization are lost hydrolysis and denaturation?
In 3-6 well developed sentences answer the question: What are the four steps for the production of a protein? What happens in each of these steps that leads to the structure of a functional protein.
Describe the two types of secondary structure apolypeptide can attain. Which proteins can achievequaternary structure? Which protein structure(s) are alteredby denaturation?
What are the four levels of protein structure, and what is the distinguishing feature of each?
How does a highly acidic solution denature proteins? A. The excess protons interfere with a protein’s ability to form peptide bonds. B. The lack of protons interferes with a protein’s ability to form peptide bonds. C. The lack of protons interferes with a protein’s ability to form secondary structures. D. The excess protons interfere with a protein’s ability to form secondary structures.

SEE MORE QUESTIONS

Recommended textbooks for you

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

Human Biology (MindTap Course List)

Biology

ISBN:

9781305112100

Author:

Cecie Starr, Beverly McMillan

Publisher:

Cengage Learning

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

Human Biology (MindTap Course List)

Biology

ISBN:

9781305112100

Author:

Cecie Starr, Beverly McMillan

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS

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.