BabcockHall

Have you thought about looking at Vmax/KM? It turns out that each parameter that you examine tells a slightly different story.

It has been a long time since I looked into this; however, I am under the impression that the hydroxyproline residues, the hydroxyl groups on the side-chains form hydrogen bonds to water. For whatever reason the presence of hydroxyproline residues increases the thermal stability of collagen.

To a rough approximation, when one has 1 mg/mL of protein, the absorbance at 280 nm will be 1 AU. Obviously this depends on the protein.

I am changing my mind on one thing; it may be that the value of 1.7 mg/mL refers to the final concentration of protein, meaning the concentration after dilution. If so, then the initial concentration must be very high, possibly at or beyond the solubility limit of a particular protein. If this is a homework exercise, then whether or not the problem is realistic from the point of view of biochemistry is secondary to getting the mechanics of the problem correct IMO.

The volume of extract (2 mL) does not enter into the dilution calculation itself, but it is needed for another portion of the calculation. You need to identify the initial concentration, the initial volume, and the final volume of the dilution, in order to find the final concentration, the concentration of the diluted sample. One thing that is a little unclear from your initial post is the interpretation of 1.7 mg/mL. I think that it refers to the initial concentration, but I could be wrong.

This is a standard dilution problem. You have to show your attempt at solving the problem first.

What do you know about using Beer's law? I have a feeling that you will only be able to obtain an approximate answer, but it is better than nothing.

Is this homework? Can you tell us what you have learned or thought of, so far?

Have you thought about oxidations?

It is also important to give credit where credit is due under any circumstance.

HMG-CoA reductase catalyzes the first committed step of the biosynthesis of cholesterol and other compounds. Therefore, it is heavily regulated, and the regulation occurs by multiple mechanisms. When one considers what conditions are expected to bring about the fastest rate of cholesterol synthesis, it might be helpful to look both at the concentration of the final product cholesterol and the energy status of the cell.

Have you looked into SREBP?

In yeast pyruvate is converted into ethanol and carbon dioxide, whereas in some bacteria, pyruvate is converted into lactate. You can apply oxidation numbers of carbon to show that either of these two processes accounts for the electrons taken from one molecule of glucose in the production of 2 molecules of pyruvate.

My previous message was not edited correction (my apologies for the confusion). I meant to write: "...without varying the concentration of I." Are you working at more than one concentration of inhibitor?

The asymptote at low concentrations of I to a graph of the pseudo first order rate constant kobs vs concentration of I is kinact/Ki. It is unclear to me how you could find this number without varying . I am pressed for time right now, but I might be able to say more later.

The fate of pyruvate under anaerobic conditions depends on the organism. Your question about oxygen is also related to the fate of pyruvate, but your question is to broad to easily be answered. Is this a homework exercise?

https://www.mitegen.com/learn/technotes/mosaicity/ https://journals.iucr.org/d/issues/2005/06/00/ic5050/ I know just enough about this subject to be dangerous. However, from what I have read the process of flash cooling can increase the mosaicity of a protein crystal. I also found this of interest from the second link: "The mosaicity provides a simple measurement of crystal quality independent of many experimental parameters. It has been used to characterize successfully the improvement seen in some microgravity samples i.e. a reduction in the reflection mosaic spread providing a corresponding increase in the signal-to-noise ratio of the reflection..."

What search engines and which search terms have you tried? You can limit PubMed searches to just reviews if you like.

Please show us what you have worked out so far.

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

My working hypothesis is that each protein might be expressed in slightly different amounts. Each ribosome binding site might be different, for example. However, I have only done a little reading on this subject.

Your structure of ethylenediamine is incorrect. Remember the Lewis octet rule.

What do you mean by placement of the N, and why do you think it might be important?

@OP, The Williamson ether synthesis is usually given as an example of SN2 chemistry in introductory organic chemistry. Aryl bromides or aryl iodides are unreactive in SN2 reactions. Why do you suppose that is the case?

My understanding of the Ullmann reaction is limited, but it appears to be a way to make biaryl compounds. Relative to what you want, the product is missing the oxygen. Can you explain why you think that the Williamson synthesis might not work in this instance?