Exam 3: Protein Structure and Function

In solution,why do hydrolysis reactions occur more readily than condensation reactions?

The aquaporin family of proteins plays a major role in the transport of water all over the body.During the folding process of these proteins,α-helices start forming as

What type of interaction is directly responsible for the formation of secondary structure?

A series of hydrophobic side chains will congregate together as a protein folds in an aqueous solution and be stabilized by

At the pH found in cells (about 7.0),what happens to the amino group on an amino acid?

Several of the molecules called vitamins act as enzyme cofactors.Vitamin deficiencies cause disease.What is the most direct explanation for this?

What prediction does the chemical evolution hypothesis make?

You have isolated a previously unstudied protein,identified its complete structure in detail,and determined that it catalyzes the breakdown of a large substrate.You notice it has two binding sites.One of these is large,apparently the bonding site for the large substrate;the other is small,possibly a binding site for a regulatory molecule.What do these findings tell you about the mechanism of this protein?

Refer to the following paragraph and figure 3.1 to answer the following questions. Figure 3.1 Since structure correlates so well with function, biochemists are constantly looking for new ways to probe the complex structure of proteins in order to understand what they do and how they do it. One of the most powerful techniques in existence today is X-ray crystallography. The main difficulty with this technique is getting the protein to crystallize. Once crystallized, the protein is bombarded with X-rays to create a pattern that can be analyzed mathematically to determine the three-dimensional structure of the protein. This analysis has been performed by Krzysztof Palczewski on the protein rhodopsin, which is a light-sensitive protein found in species ranging from ancient bacteria (archaea)to humans. The structure (schematically shown above, where each letter represents an amino acid)is characterized by a single polypeptide chain with several α-helical segments that loop back and forth across the cell membrane. Another notable feature is the disulfide bond (-S-S-)that can be seen at the bottom of the third transmembrane segment. [Figure adapted from K. Palczewski et al., Science 289 (2000): 739.] -If you were reading off the sequence of amino acids in Figure 3.1 to a biologist friend,what should the first three letters be?

When,and by whom,was the lock-and-key model of enzyme specificity developed?

Which one of the following is not a component of each monomer used to make proteins?

Refer to the following paragraph and figure 3.1 to answer the following questions. Figure 3.1 Since structure correlates so well with function, biochemists are constantly looking for new ways to probe the complex structure of proteins in order to understand what they do and how they do it. One of the most powerful techniques in existence today is X-ray crystallography. The main difficulty with this technique is getting the protein to crystallize. Once crystallized, the protein is bombarded with X-rays to create a pattern that can be analyzed mathematically to determine the three-dimensional structure of the protein. This analysis has been performed by Krzysztof Palczewski on the protein rhodopsin, which is a light-sensitive protein found in species ranging from ancient bacteria (archaea)to humans. The structure (schematically shown above, where each letter represents an amino acid)is characterized by a single polypeptide chain with several α-helical segments that loop back and forth across the cell membrane. Another notable feature is the disulfide bond (-S-S-)that can be seen at the bottom of the third transmembrane segment. [Figure adapted from K. Palczewski et al., Science 289 (2000): 739.] -What is the location of the C-terminus of the protein in Figure 3.1?

At the pH found in cells (about 7.0),what happens to the carboxyl group on an amino acid?

Refer to the following paragraph and figure 3.1 to answer the following questions. Figure 3.1 Since structure correlates so well with function, biochemists are constantly looking for new ways to probe the complex structure of proteins in order to understand what they do and how they do it. One of the most powerful techniques in existence today is X-ray crystallography. The main difficulty with this technique is getting the protein to crystallize. Once crystallized, the protein is bombarded with X-rays to create a pattern that can be analyzed mathematically to determine the three-dimensional structure of the protein. This analysis has been performed by Krzysztof Palczewski on the protein rhodopsin, which is a light-sensitive protein found in species ranging from ancient bacteria (archaea)to humans. The structure (schematically shown above, where each letter represents an amino acid)is characterized by a single polypeptide chain with several α-helical segments that loop back and forth across the cell membrane. Another notable feature is the disulfide bond (-S-S-)that can be seen at the bottom of the third transmembrane segment. [Figure adapted from K. Palczewski et al., Science 289 (2000): 739.] -Which term best describes the protein in Figure 3.1?

Which of the following observations is the strongest argument in favor of the hypothesis that protein structure and function are correlated?

Suppose that Miller repeated his chemical evolution experiment,but without a source of electrical sparks.What would be the purpose?

Which one of the following is not a component of each monomer used to make proteins?

Refer to the following paragraph and figure 3.1 to answer the following questions. Figure 3.1 Since structure correlates so well with function, biochemists are constantly looking for new ways to probe the complex structure of proteins in order to understand what they do and how they do it. One of the most powerful techniques in existence today is X-ray crystallography. The main difficulty with this technique is getting the protein to crystallize. Once crystallized, the protein is bombarded with X-rays to create a pattern that can be analyzed mathematically to determine the three-dimensional structure of the protein. This analysis has been performed by Krzysztof Palczewski on the protein rhodopsin, which is a light-sensitive protein found in species ranging from ancient bacteria (archaea)to humans. The structure (schematically shown above, where each letter represents an amino acid)is characterized by a single polypeptide chain with several α-helical segments that loop back and forth across the cell membrane. Another notable feature is the disulfide bond (-S-S-)that can be seen at the bottom of the third transmembrane segment. [Figure adapted from K. Palczewski et al., Science 289 (2000): 739.] -Identify the location of the disulfide bond in Figure 3.1.What is the name of the amino acids that are forming this bond?

If the primary structure of a protein is incorrect

Which of the following best describes primary structure in proteins?