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HW#2 - were calculated 3 What are the major findings(i.e...

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Jin Bae Bio 501 Research Paper Questions 1. What is the hypothesis/question driving this work? The question regarding to the experiments done by Whitney and Tanford is looking at the effects of aqueous urea on protein denaturation, and testing the solubility of amino acids in urea solutions. The idea that supports the stability of globular structure in water and its instability in urea is based on the fact that hydrogen bonds between one peptide group and another are generally stronger than its interaction with water. However, there are strong indications that hydrogen bonds between peptide groups are in fact not significantly stronger than hydrogen bonds involving water. What is the role of urea in the denaturing process? 2. What experimental approaches were used to test the hypothesis? Measuring the solubility of several amino acids with predominant non- polar side chains in aqueous urea solutions and water. Free energies transfer of amino acid side chains and backbone peptide units from water to the solutions
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Unformatted text preview: were calculated. 3. What are the major findings (i.e., results)? The figures in Table I account for the denaturing action of 8 M urea. The tyrosine side chain seems to be slightly more hydrophobic than the phenylalanine side chain. 40% ethanol and 7 M urea produce about an equal extent of unfolding. The 8 M urea is to some extent more complete. 4. What are the major conclusion(s)? Aqueous urea solutions accommodate non-polar side chains of amino acids more readily than water does. The constituent parts of the amino acid molecule interact with the solvent independently. Urea solutions are better at solubilizing aromatic side chains, such as phenylalanyl and tyrosyl groups. 5. What points about the paper are confusing or unclear? I do not really understand the experiment behind the process of measuring the solubility of different amino acids. Also, the calculation behind finding the free energy is confusing....
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