The following questions are in regards to (2BRD) CRYSTAL STRUCTURE OF BACTERIORH
ID: 71607 • Letter: T
Question
The following questions are in regards to (2BRD) CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN PURPLE MEMBRANE
To help answering the questions visit Protein Database entry in the link below:
http://www.rcsb.org/pdb/explore/explore.do?structureId=2brd
Q1) Which of the following statements is consistent with the composition of the alpha helices in 2BRD?
1. The alpha helices are composed mostly of nonpolar amino acids.
2. The alpha helices are composed mostly of polar amino acids.
3. The alpha helices are composed of alternating nonpolar and polar amino acids.
4. The alpha helices show no ordered arrangement of the amino acids.
Q2) In 2BRD, what type of noncovalent interaction is likely occurring between Ile 191 and the closest lipid molecule?
1. hydrogen bond
2. ion pair
3. dipole-dipole interaction
4. London dispersion forces (induced dipole-induced dipole interactions)
Q3) Which of the following statements best describes the hydrophobic character of bacteriorhodopsin (2BRD)?
1. Both the interior and exterior of the protein are hydrophobic, including the central core of the trimer.
2. Both the interior and exterior of the protein are hydrophobic, but the central core of the trimer is hydrophilic. 3. Both the interior and exterior of the protein are hydrophilic, including the central core of the trimer.
4. Both the interior and exterior of the protein are hydrophilic, but the central core of the trimer is hydrophobic.
Explanation / Answer
1. As seen in the link given inthe question, alpha helices mainly composed of hydrophobic region. Thus, is made up of mainly of nonpolar amino acids which are hydrophobic in nature.So the answer is..
The alpha helices are composed mostly of nonpolar amino acids.
2. The answer is London dispersion forces (induced dipole-induced dipole interactions)
3. Both the interior and exterior of the protein are hydrophilic, including the central core of the trimer.
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