Consider the following statement. “To produceone molecule of each possible kind of polypeptide chain,300 amino acids in length, would require more atoms thanexist in the universe.” Given the size of the universe, do yousuppose this statement could possibly be correct? Sincecounting atoms is a tricky business, consider the problemfrom the standpoint of mass. The mass of the observableuniverse is estimated to be about 1080 grams, give or takean order of magnitude or so. Assuming that the averagemass of an amino acid is 110 daltons, what would be themass of one molecule of each possible kind of polypeptidechain 300 amino acids in length? Is this greater than themass of the universe?

Consider the following statement. “To produceone molecule of each possible kind of polypeptide chain,300 amino acids in length, would require more atoms thanexist in the universe.” Given the size of the universe, do yousuppose this statement could possibly be correct? Sincecounting atoms is a tricky business, consider the problemfrom the standpoint of mass. The mass of the observableuniverse is estimated to be about 1080 grams, give or takean order of magnitude or so. Assuming that the averagemass of an amino acid is 110 daltons, what would be themass of one molecule of each possible kind of polypeptidechain 300 amino acids in length? Is this greater than themass of the universe?

Principles Of Pharmacology Med Assist

6th Edition

ISBN:9781337512442

Author:RICE

Publisher:RICE

Chapter3: Ratio And Proportion

Section: Chapter Questions

Problem 5PP

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Hundreds of thousands of proteins have been discovered inliving organisms. Yet, as astonishing as this diversity is,these molecules constitute only a small fraction of thosethat are possible. Calculate the total number of possibledecapeptides (molecules with 10 amino acid residues linkedby peptide bonds) that could be synthesized from the 20standard amino acids. If you were to spend 5 minutes writing out the molecular structure of each possible decapeptide,how long would the task take?
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 0.0916 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.
Assume that some protein molecule, in its folded native state, has onefavored conformation. But when it is denatured, it becomes a “random coil,” with many possible conformations.(a) If we only consider the change in entropy for the protein, what mustbe the sign of ΔS for the change: native → denatured? (Note: As suggestedin the next problem, this does not include solvent effects, which also make significant contributions to ΔS.)(b) How will the contribution of ΔS for native → denatured affect thefavorability of the process? What apparent requirement does this imposeon ΔH if proteins are to be stable structures?
Two common methods of denaturing proteins in the lab are to increase the temperature and/or add chemical denaturants like the detergent SDS (shown below). Describe how each of these processes (heating and addition of SDS) disrupts the forces and interactions that stabilize the native state, leading to unfolding. The answer should include a discussion of the Gibbs free energy of folding, enthalpy, and entropy.
Consider a small protein containing 101 amino acid residues. The proteinbackbone will have 200 bonds about which rotation can occur. Assume thatthree orientations are possible about each of these bonds.(a) Based on these assumptions, about how many random-coil conformationswill be possible for this protein?(b) The estimate obtained in (a) is surely too large. Give one reason why.
Which of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…
Consider two proteins, A and B, that can interact with a Ka = 2.55 nM. If you mix the two proteins so that their initial concentration are [A] = 0.10 nM and [B] = 3.0 nM, what percentage of free A do you expect to observe after the solution reaches the equilibrium? 85% 33% 46% 54%
In an ESI spectrum, you see a peak at m/z = 1293.51. You know that peak corresponds to a charge of +10. What is the mass of the protein, in kDa? 14.4 33.6 O 12.9 15.8
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