BabcockHall

One more thing for protein helices. I would ask what are the values of the dihedral angles, phi and psi, and whether or not they fall into the allowed region of the Ramachandran diagram.

I don't know the answer to this question, but the kinds of questions I would ask about any helix would be handedness, hydrogen bonding patterns, and translation of the helix per unit residue.

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Hello Everyone, I am making enzyme inhibitors and turning them over to a microbiology laboratory for testing against standard strains of bacteria and fungi. They are performing disk diffusion assays, and seeing a few results that look positive. I would like better to understand the meaning and limitations of this experiment. I would hazard a guess that the compound's concentration falls off at greater distances from the disk, but I don't know how to interpret the diameter of the dead zone in a quantitative way, or even if that is possible. Perhaps there is a good textbook treatment of this subject, for example.

Please show your attempt. If you can, please explain where you got stuck.

I can't say which transition state without knowing the other reactants besides oxygen. Let me limit myself to nucleophilic substitution reactions for the sake of illustration. By an open transition state I mean one in which the leaving group has largely left (the bond order to the central atom might be roughly 0.2) and the nucleophile is only weakly present (bond order also might be around 0.20). The opposite situation (a tight transition state) is one in which the leaving group has just begun to depart (bond order of 0.8 or so) and the nucleophile has largely made a bond to the central atom.

Dissociative or associative might be applied to the nature of the transition state. Dissociative means that the transition state is open (exploded), and associative means the opposite.

Did you try using the Henderson-Hasselbalch equation?

As a general rule B. subtilis does chemotaxis in a different (sometime opposite) way versus E. coli. I never thought about bushings before, but I will ask around.

When an enzyme is saturated with its substrate, its velocity reaches its maximum, notated as Vmax. Because enzymes are catalytic and because one has different purposes, it is not possible to give a general answer about how much enzyme to use in a given experiment. When discussing the quantity of enzyme, one often encounters the word "unit." One unit of an enzyme is the amount that will convert one micromole of substrate to product per minute under a given set of conditions. Often enzymes are sold on the basis of how many units are present.

I am not sure that a transporter in the outer membrane would be needed, owing to the presence of porins in the outer membrane.

Ciak, What if you used a molecule with two different halogens at the 1 and 3 positions?

Is this homework?

Is this a homework problem or an exam problem? Can you explain what you were taught and what you do and don't understand at this point?

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Can the aromatic ring stabilize a putative carbocation (assuming it goes SN1)? A drawing may be helpful.

@OP, What makes a substrate a good candidate for the SN1 process? for the SN2 process? Once you are sure of these answers, look at the substrate of this problem.

@OP, In general please show your work or give your thoughts in your first post. Substitutions reactions at a benzylic carbon might go one way or the other, depending on additional factors. The degree of substitution of the carbon and the hydroxy substituent on the aromatic ring (assuming it is present) are both factors here. Why don't you provide your thoughts now?

@OP, If you have a sodium as a countering, what does that suggest about the rest of the reagent?

That might be the product. The starting material is a triacylglycerol.

Do you recognize the starting material or the alcohol?