BabcockHall

What are your thoughts? Once you provide your ideas, someone may be able to help you.

Do you mean triglyceride? If so, then what do you think of the relative polarities of a triglyceride and a typical phospholipid?

It has been many years since I studied freezing of glycerol solutions. IIRC at about 67% glycerol, one never actually sees freezing, but instead one gets a glass. There is some good literature out there because of electron microscopy, low temperature EPR studies (EPR spectroscopists prefer glasses), and crocrystallography. It took me a while to tap into it, though.

Is this homework? Do you know what the definition of activity is?

Would you mind defining your abbreviations? They are not familiar to me.

Acid-base chemistry is important in organic, and some students really struggle with it. Therefore, I would say that winter break is a great time to nail the basics completely.

Would you care to define polarizability for us?

The size and composition of the meal are probably factors which go into how quickly the stomach empties a given meal.

Meaning to say, evolution can be determined by fossils? And where can we find fossils? How would they know that what they have is already a fossil?Thank you sir for your reply.

There are also DNA sequences of the same protein in different organisms, for example.

Well, your first comment was all about how I use the definition wrong, without even trying to explain yourself, so I can't see any helping with leaving a comment that says "You are wrong".

Thanks for the definition tho, but it's still not clear to me how the PKa is effected from the electronegativity.

Your opening post was poorly formatted and had no pK_a values or names of amino acids. When it was pointed out to you that your understanding of electronegativity was wrong, you should have looked it up yourself. Helping someone is not the same as doing their work for them.

I don't need electrostatics in high level, just some principles in biochemistry.

I didn't say all amino acids, the question is about positive charge amino acids (those that have epsilon amino in the R group), my definitions might be a little wrong but I think I'm clear.

And I'm here to understand things better, and not for someone to tell me how wrong I am, so thanks for nothing.

If anyone else could explain this to me I would be very thankful

The three amino amino acids with positively charged side-chains have very different structures, and for that reason alone, attempting to explain all of their values with one single concept is unlikely to lead to success. With respect to the ammonium groups in amino acids both electronegativity and electrostatics are factors (although it might make sense to start with electronegativity).

addendum: doublet from structure 1 is from t-butyl

No, the H's would not couple. n is 1 due to the t-butyl because the distance is 2 bonds.

Explain structure 3 to me, please.

Between the hydrogen atoms of the t-butyl group and the hydrogen in question there are four bonds, not two bonds. When there are four bonds, the coupling constant is usually small and may be undetectable.

Get a plastic model kit for organic chemistry. It can be difficult to visualize organic molecules in three dimensions, but a good model kit can help immensely.

Electronegativity concerns electrons being potentially shared in a covalent or other kind of bond. Electron affinity is a measure of the change in energy when an atom gains an electron; therefore, it could be thought of as how much an atom wants to gain an electron. I was thinking of low-level electrostatics. Pro tip: being rude to people who are trying to help you is not a winning strategy.

But how many were pay-per-view?

 

28 of 88 reviews were "free full text." You can ask Pubmed to give you this option. Here is one example:

14-3-3 proteins as potential therapeutic targets.

n-1

Gamma Girl,

Your answer does not make any sense. What is n? Also it seems to me that you may be confusing rules that govern splitting with rules that govern the integration of peaks.

With respect to the question that I asked, the answer is that hydrogen atoms that are connected by two or three bonds show coupling that is typically easily seen. Hydrogen atoms connected by four or more bonds couple with each other with such small coupling constants that it is often difficult or impossible to detect. Unless your instructor told you otherwise, it is probably a safe bet that coupling between hydrogen atoms that are separated by four or more bonds can be ignored.

What were you taught with respect to the number of bonds that connect two atoms that show coupling?

Your definition of electronegativity is misleading, and not all amino acids have an amino group at the epsilon position. I would focus on electrostatics.

I went to Pubmed, searched "14-3-3 protein cancer" and I limited my search to review articles. I found 88 citations that way.

What did you find out about the metabolism of leucine?

Surface-exposed loops, by contrast, are sometimes more accessible to proteases.

What two functional groups do these two compounds have in common with each other?

One way to think about gas chromatography is that it separates molecules on the basis of their relative tendencies to be in the gas phase versus a particular liquid phase. What can the experimenter do to affect this partitioning?

The obvious answer is that there is no glycogen left, but I recall that it proceeds more slowly with time during a fast.

 

An abundance of blood glucose would be expected to stop glycogenolysis in the liver. Therefore, one should look at how insulin regulates the key enzymes.

Please post your best attempts at answers or your thoughts, and then perhaps someone can respond.

I am pretty familiar with anion-exchange and cation-exchange, but what are P and Mo? Do you mean the elements phosphorus and molybdenum, or something else?