BIOL 190 Study Guide - Midterm Guide: Guanine, Ribose, Nitrogenous Base

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copperwoodchuck239

7 Oct 2016

School

University of San Diego

Department

Biology Courses

Course

BIOL 190

Professor

Leavitt, Dean

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Document Summary

How does the 3-d structure of a protein arise from its primary sequence: order of amino acids determines how and where it bends to form bonds between amino acid side chains. This then dictates how a protein folds to keep hydrophobic molecules away from water. What do secondary, tertiary, and quaternary structure refer to: tertiary - the folding of a protein to keep hydrophobic molecules away. Secondary - the bonding of amino acids to neighboring amino acids from water: quaternary - how a polypeptide is combined with other polypeptides to make a complete protein. A denatured protein loses shape, and therefore losses functionality. Chaperonin proteins store polypeptides during the folding process to ensure that the polypeptide folds properly nucleotide. Pass on genetic material: control functions of a cell. What was rosalind franklin"s contribution to deciphering the structure of. Xray technician who took photos of dna for crick and watson.

Related Questions

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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The linear sequence of amino acids is referred to as the primarylevel of protein structure. However, the primary sequence affectsall other aspects of protein structure.

a. Explain how an amino acidchange outside of the active site of a particular enzyme couldaffect the function of that enzyme. (2pts)

b. Explain how that same aminoacid change could have no affect on the function of the enzyme.(2pts)

c. Imagine a protein in which acysteine is converted to a serine. How would this mutation affectthe secondary, tertiary and quaternary structure? (3pts)

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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.

BIOL 190 Study Guide - Midterm Guide: Guanine, Ribose, Nitrogenous Base

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