Proteins frequently form complexes in which 2, 3, 4, or even more individual proteins ("monomers") interact specifically with each other via hydrogen bonds or electrostatic interactions. The entire assembly of proteins can act as one unit in solution, and this assembly is called the "quaternary structure" of the protein. Suppose you discover a new protein whose monomer molar mass is 25,000 g/mol. You measure an osmotic pressure of 0.122 atm at 37 °C for 7.20 g of the protein in 10.00 mL of an aqueous solution. How many protein monomers form the quaternary protein structure in solution? Treat the protein as a nonelectrolyte. 6 5 3 0.4 2

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Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
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Chapter1: Chemical Foundations
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Proteins frequently form complexes in which 2, 3, 4, or even more individual proteins
("monomers") interact specifically with each other via hydrogen bonds or electrostatic
interactions. The entire assembly of proteins can act as one unit in solution, and this
assembly is called the "quaternary structure" of the protein. Suppose you discover a new
protein whose monomer molar mass is 25,000 g/mol. You measure an osmotic pressure of
0.122 atm at 37 °C for 7.20 g of the protein in 10.00 mL of an aqueous solution. How many
protein monomers form the quaternary protein structure in solution? Treat the protein as a
nonelectrolyte.
C
6
O
5
3
0.4
2
Transcribed Image Text:Proteins frequently form complexes in which 2, 3, 4, or even more individual proteins ("monomers") interact specifically with each other via hydrogen bonds or electrostatic interactions. The entire assembly of proteins can act as one unit in solution, and this assembly is called the "quaternary structure" of the protein. Suppose you discover a new protein whose monomer molar mass is 25,000 g/mol. You measure an osmotic pressure of 0.122 atm at 37 °C for 7.20 g of the protein in 10.00 mL of an aqueous solution. How many protein monomers form the quaternary protein structure in solution? Treat the protein as a nonelectrolyte. C 6 O 5 3 0.4 2
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