Lecture : Bio Notes 202 - Proline

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azaillia

30 Mar 2023

School

UCF

Department

Biology

Course

BSC 2010C

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Document Summary

Proline is one of the 20 amino acids that make up proteins and is classified as a non-essential amino acid, meaning that it can be synthesized in the body. It has a unique structure compared to other amino acids, with a side chain that is covalently bonded to the nitrogen of the amino group, creating a cyclic structure. Proline"s chemical formula is c5h9no2, and its unique structure affects its properties and functions. It is commonly found in the collagen protein, where its rigid cyclic structure helps maintain the stability and structure of collagen fibers. It is also found in the active sites of enzymes and in certain signal transduction pathways in the cell. In addition to its role in protein synthesis and structure, proline has been found to play a role in wound healing and immune response.

Related Questions

1. The level of protein structure that is stabilized primarilyby non-covalent interactions between the side chains within asingle polypeptide chain is refered to as its:

A) primary structure

B) secondary structure

C) tertiary structure

D) quaternary structure

E) none of the above

2. Collagen, a strong fibrous protein found in connectivetissue, bone, and the extracellular matrix, has a structure inwhich three left-handed helices wind around each other to form aright-handed triple helix. The primary structure of collagen has arepeat unit of -(Gly-X-Pro)- Which of the following bonds stabilizethe collagen triple helix? (mark all that apply)

A) Hydrogen bonds between hydroxyproline residues

B) Hydrogen bonds between N-H and C=O

C) Ionic bonds between amino acid side chains

D) Hydrogen bonds between charged amino acids

3. The non-covalent forces that stabilize the Beta-strandconformation of peptides include:

A) H-bonds between amide C=O and amide NH

B) Van der Waals packing between the peptide backbone atoms

C) Van der Waals packing due to side chain interdigitation

D) Only A and B above

E) None of the above

4. What is the approximate length difference of a 22-kDasingle-stranded ?-helical protein segment vs. a 22-kDasingle-stranded ?-strand protein segment? Assume a mean residuemass of 110 Da. Show work.

5. Circular dichroism measurements have shown that the peptidebackbone of poly-l-lysine (KKKKKKK) adopts a random coilconformation at pH 7.0, but becomes ?-helical as the pH is raisedabove 10. This observation is known as the

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What roles do proteins play in cells?

What are the monomers of proteins? Describe their basic structure.

What does the nature of the side chains (R groups) of amino acids suggest about their basic position in membrane proteins? What about in the cytoplasm? Or in the bloodstream?

Specifically how are amino acids linked together?

What is the primary structure of a protein? How is it determined?

Describe the interactions between amino acids that contribute to form the secondary structure of a protein. What are some of the basic configurations that result?

Describe the interactions between amino acids that form the tertiary structure of a protein.

What is the quaternary structure of a protein? Is this always a feature of protein structure?

Describe the role of chaperonins (chaperone proteins) in determining the final structure of a protein. Why are these chaperones necessary?

Use text Figure 5.19 to discuss the importance of protein structure in determining function. Be sure to use the vocabulary relevant to this topic in your discussion.

The sequence of amino acids is considered to be the ________ structure of a protein.

Select one:

a. secondary

b. tertiary

c. quaternary

d. primary

The pattern the backbone folds, for example alpha-helix or beta pleated sheet, is the ________ structure of a protein.

Select one:

a. quaternary

b. secondary

c. tertiary

d. primary

Which type of forces stabilizes the primary structure of a protein?

Select one:

a. Salt bridges

b. Hydrogen bonding between the carbonyl group and amino group

c. Dipole-dipole

d. Peptide bonds

The interaction of the side chains on the amino acids, for example hydrophobic attractions, is the ________ structure of a protein.

Select one:

a. quaternary

b. secondary

c. tertiary

d. primary

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Lecture : Bio Notes 202 - Proline

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