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 structu proteins in order to understand what they do and how they do it. One of the most powerful techniques in existence today is X 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
a- 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?
A) cytosine
B) glycine
C) cysteine
D) aspartic acid
Correct Answer:
Verified
Q19: An amino acid has an R- group
Q20: Why are polymerization reactions endergonic?
A) They release
Q21: You have isolated a previously unstudied protein,
Q22: You've just sequenced a new protein found
Q23: Refer to the following paragraph and Figure
Q25: What type of interaction is directly responsible
Q26: Which of the following best describes primary
Q27: When, and by whom, was the lock-
Q28: Recent technological advances have made it more
Q29: If the primary structure of a protein
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