DOING THE CROSSWORD PUZZLE INSTEAD OF TAKING NOTES IN CLASS IS A BAD IDEA.
I'm going to fail and it's all my fault. *sob!*
Seriously. If your classes and labs, which cost many thousands of dollars, can't distract you from your newspaper, which costs one dollar, it's time to reconsider your investments.Keffria wrote:O_o
Well, then. Perhaps it's time to switch to something that interests you enough to distract you from the newspaper?

Most of this is way beyond my knowledge of chemistry too. But I can maybe give you a nudge in the right direction...Tellurider wrote:"The redox potential of a metalloprotein reflects ist conformational state. The following table presents circular dichroism (CD) ellipticities (theta) for reduced (Fe2+ heme) and oxidized (Fe3+ heme) cytochrome c as a function of chemical denaturant concentration ([GdmHCl]) at 40 degrees C. The CD signal essentially measures the degree of secondary structure found in the protein. At low [GdmHCl] the protein is completely folded, at high GdmHCl it is denatured. Take theta as a probe of this transition.
a) With the data below find the difference in redox potential between the folded and unfolded states. (Hints: make use of the Gibbs equation and the Nernst equation to relate the equilibrium constant for folding at 0 M GdmHCl to the redox potential. Think in terms of a closed thermodynamic cycle of the states available to the protein)
b) What does the change in redox potential on unfolding (and/or differential stability of oxidized vs. reduced) tell you about the environment of the heme in the native state of this protein (Note that the porphyrin ring itself is dibasic)
Aw, man, not another one!rkolter wrote:I am kind of surprised by his absence from this thread. C'mon Lego - tell us a story about protein folding, electronegativity, and the free energy equation.phactorri wrote:I bet Lego could rock this stuff out.