1. What are the levels of protein structure? 2. What is the role of myoglobin and...
1. What are the levels of protein structure?
2. What is the role of myoglobin and describe the levels of protein
structure that exists in myoglobin using PyMOL?
3. What types of forces exist to keep a protein in its native
state?
4. What is denaturation? And describe some of the agents that cause
denaturation.
Homework Answers
Ans 1- Proteins are biological polymers composed of amino acids.
Amino acids, linked together by peptide bonds, form a polypeptide
chain.
Add Answer to:
1. What are the levels of protein structure?
2. What is the role of myoglobin and...
4. (a) Define the four levels of protein structure (primary, secondary, tertiary, and quaternary). (2 pt)...
4. (a) Define the four levels of protein structure (primary, secondary, tertiary, and quaternary). (2 pt) (b) List four examples of types of interactions which give rise to tertiary structure. (2 pt) (c) What is protein denaturation, and list at least three ways this can be achieved. (2 pt)
Test your understanding of the term denaturation by deciding which of the following statements are true....
Test your understanding of the term denaturation by deciding which of the following statements are true. 1.Denaturation of an enzyme will cause a loss of its catalytic activity 2.Denaturation and digestion refer to the same process 3.A competitive enzyme inhibitor acts by denaturing the enzyme 4.Protein denaturation involves cleavage of its peptide bonds 5.A denatured protein has a different tertiary structure than its native state 6.A denatured protein has a different primary structure than its native state
a) What aspects of protein structure and folding are explained by entropy? How does entropy affect...
a) What aspects of protein structure and folding are explained
by entropy? How does entropy
affect a protein’s native versus denatured structure?
b) What aspects of protein structure and folding are explained
by enthalpy? How does enthalpy
affect a protein’s native versus denatured structure?
c) What aspects of protein structure and folding are
illustrative of equilibrium (or disequilibrium)?
1. The figure below shows the physical representation of a native protein versus a denatured protein 72 native state A-state 23 17...
Which one or more of the four hierarchical levels of protein structure is/are always lost during...
Which one or more of the four hierarchical levels of protein
structure is/are always lost during protein denaturation?
* I know the answer is tertiary but want to know why?
My uni gave me this table below but I don't know why the answer
is then teriary(they gave this answer). Can someone please
explain.
*
On what structural features does the catalytic activity of an enzyme depend? (1) Definition:"Enzyme denaturation" loss of enzyme structure, (almost) always with loss of biological...
1. What are the different types of proteins and their function? 2. Explain the meaning and importance of the primary, secondary, tertiary and quaternary structures of a protein and the factors that...
1. What are the different types of proteins and their function? 2. Explain the meaning and importance of the primary, secondary, tertiary and quaternary structures of a protein and the factors that cause its denaturation.
6.) Provide short answers for the questions about protein structure below: a.) True or False, amino...
6.) Provide short answers for the questions about protein structure below: a.) True or False, amino acid sequence defines the native structure of protein. b.) What is the main type of bonding responsible for stabilizing the secondary structure of proteins? c.) Briefly discuss the thermodynamics of protein folding into its native 3D structure. Is this process enthalpy driven or entropy driven? d.) Give an example of 2 major secondary structural motifs found in polypeptides. Do any of these motifs appear...
biochem quest. Each of the following reagents or conditions will denature a protein. For each, describe what the re...
biochem quest.
Each of the following reagents or conditions will denature a protein. For each, describe what the reagent/condition does to interrupt the native protein structure. (a) temperature (c) detergent (d) extreme pH. Show a melting curve ofa protein - label the Tm and indicate on your graph whether the protein is found in its native structure or in a denatured state. (8 points) (b) high urea
Each of the following reagents or conditions will denature a protein. For each,...
1. Contrast the structure and function of myoglobin and hemoglobin. Describe the primary, secondary, tertiary and...
1. Contrast the structure and function of myoglobin and hemoglobin. Describe the primary, secondary, tertiary and quaternary structure of both proteins. Describe their motifs and domains if appropriate. 2. How similar are the mammalian hemoglobin and myoglobin (in terms of amino acid composition)? 3. Recall the functions and structure of leghemoglobins, chlorocruorins, hemerythrin and hemocyanin. In what organisms are those proteins found? How are this globins different from mammalian globins? 4. Not all O2 molecules bind to each of the...
Describe the four levels of protein structure. What are the similarities and differences between DNA and...
Describe the four levels of protein structure. What are the similarities and differences between DNA and RNA?
Lumpur QUESTION 2 Myoglobin is a globular protein. About half of its 153 amino acids have...
Lumpur QUESTION 2 Myoglobin is a globular protein. About half of its 153 amino acids have nonpolar side chains. Where would you expect those amino acids to be located in the tertiary structure? Inside the compact tertiary structure Outside the compact tertiary structure Evenly distrubuted On the edges of the amino acids primary chain QUESTION 3 What type of bonding is responsible for the primary structure of a protein? covalent bonds hydrogen bonds ionic bonds alpha helices
a) What aspects of protein structure and folding are explained
by entropy? How does entropy
affect a protein’s native versus denatured structure?
b) What aspects of protein structure and folding are explained
by enthalpy? How does enthalpy
affect a protein’s native versus denatured structure?
c) What aspects of protein structure and folding are
illustrative of equilibrium (or disequilibrium)?
1. The figure below shows the physical representation of a native protein versus a denatured protein 72 native state A-state 23 17...
Which one or more of the four hierarchical levels of protein
structure is/are always lost during protein denaturation?
* I know the answer is tertiary but want to know why?
My uni gave me this table below but I don't know why the answer
is then teriary(they gave this answer). Can someone please
explain.
*
On what structural features does the catalytic activity of an enzyme depend? (1) Definition:"Enzyme denaturation" loss of enzyme structure, (almost) always with loss of biological...
biochem quest.
Each of the following reagents or conditions will denature a protein. For each, describe what the reagent/condition does to interrupt the native protein structure. (a) temperature (c) detergent (d) extreme pH. Show a melting curve ofa protein - label the Tm and indicate on your graph whether the protein is found in its native structure or in a denatured state. (8 points) (b) high urea
Each of the following reagents or conditions will denature a protein. For each,...
Describe the four levels of protein structure. What are the similarities and differences between DNA and RNA?
Lumpur QUESTION 2 Myoglobin is a globular protein. About half of its 153 amino acids have nonpolar side chains. Where would you expect those amino acids to be located in the tertiary structure? Inside the compact tertiary structure Outside the compact tertiary structure Evenly distrubuted On the edges of the amino acids primary chain QUESTION 3 What type of bonding is responsible for the primary structure of a protein? covalent bonds hydrogen bonds ionic bonds alpha helices
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