Bluenoise

Uhh fluidity of what? lol

Right but the bonus about desinging a catalytic antibody to the transition state of the reaction is that it comes with a substrate binding site that is already catalytic for the reaction.

Right but since they both existed before either mitochondria or chloroplast the heterotrop hypothesis does nothing to answer the question. Anyways I voted same as you guys, since it's more likely. I'm trying to get some alternative opinions.

"heterotroph hypothesis" That gives the order of emergence of heterotrophs and photosyntetic bacterium. Neither of which contain mitochondria or chloroplasts...

I'm currently studying Biochemistry with a molecular biology option. Yes I know, lots of biology like everyone else. But Dammit it's what I've always wanted to do. I swear I'm not in it for the money, hell there are better ways to make it. At the age of 7 I was already making experiments, growing shit, and trying to make explosives etc... I'm currently working on interations between various NOS isozymes and Calmodulin. However I intend to end up doing work involving protein engineer, or maybe studying protein interations involved in gene expression. Biochemistry is definatley a good feild to go into if you're interested in either chemistry or biology. If you realize early you only one to go into one or the other usually you can switch with no penalty. Or even if you graduate with a biochem degree you can do either plus many more things. Though it's definatley not one of the easier things to do in life.

It hasn't been proven either way. I have my opionion but what's your'se? p.s. (I would have posted this in the poll forum but there's so rediculousness about have to do it by correspondance to an admin, Hmmmm I wonder why there's only been 1 new poll posted in the last 3 months.) But anyways this forum is appropriate enough.

Not proven either way. What's your opinion?

What do you think about the use of catalytic antibodies to design active sites for new enzymatic reactions. Then illucidating the structure and sequence of these sites and using the data as a template for the design of catalytic sites on proteins. These would obviously have pretty low rate enhancements initially (~10^4) or so. But they could probably be increased significantly through the use of guided evolution or even maybe some inginuitive fidling. It's an idea I've been fidling with. I know it's most likely being done now already, and i'll have a look around. But I'm curious on people oppinions on the idea.

Zynods right, it's believe that many viruses originated from self copying dna sequences like transposons. Like a LTR element with an env gene is pretty much a retrovirus.

Sure you could, but the pill would be soooo big you'd choke to death trying to swallow it. Think about it a single hard candie is almost 100% sucrose you can't get energy much more condensed than that. Now they're pretty big and hard to swallow. plus 1 can't hold you out for a full day. So yeah that idea can work, but you'd be swallowing a fairly large handfull of pills a day.

Well yes it also go farther than being catalysts in enzymes. A protein them I'm researching "calmodulin" binds 4 Ca2+ atoms, which do not surve in any catayltic mechanism, but instead work to active this protein by changing its conformation and helping it to bind to other proteins like "Nitric oxide synthase" which it in itself activates. And the signals don't apply to just neurological ones many functions can be signaled by ions either defusing across cell membranes or activating receptors on these membranes. cheers

Yep they're fatal for the most part. The reason that downs syndrome only occurs on chromosome 21 is because it's the smallest chromosome (besides y) so the genetic imbalance caused by the extra copy is less than for the other chromosomes. Also chromosomes are numbered from largest to smallest 1 -> 22. Uhhh and they messed up with 22 it looks smaller than 21 but it is actually slightly bigger.

They are good for you!!!!! The problem is you're just eating tooo much since they taste so damn good!!!! And even too much of a good thing can be bad. that basically sums it up.

Well most of them function as enzyme cofactors like iron does in your example. Cu, Zn, Mg, Ca, Se, and Co are all comonly used as enzyme cofactors plus others. Some can funtion to stabalize different macromolecular assemblies, like Mg and Ca in cell membranes etc. They also function to maintain various gradients of ion concentrations that are important to drive certain processes. As well as some of them most notably Ca work as signal molecules, many important process such as muscle funtion or embryogenesis are controlled by Calcium concentration fronts.

Umm where to begin. Well it's basically the study of the chemistry of life. Looking at the chemical processes that underly biology. It generally involves alot of work with proteins. The sort of tools and techniques that are used include biochemical ones and just about everything in molecular biology. The feilds overlap greatly and often the biggest distinguishing factor is what they're looking for, not how they're searching for it. It also covers alot of varied areas leaving you with many options, you could go and do pure chemistry or biology. The types of courses you'd be taking usually involve a whole lot of varied chemistries and bology courses oriented around things like microbiology, molecular biology, fermentation, biotech etc. Plus a bunch of more biochem focuses courses which most of show up mainly in later years. Umm I don't really know what else to say. Any questions?

A racemic mixture contains equal amounts of both optical isomers. To seperate them you a reactive species that's present in only on enantiomer. This will give you two different products that you can seperate. Then you reverse the reaction.

Yeah they basically exist for the very short time it takes them to find something to react with to make a stabler arrangement

I'm not sure why they call the R part of those carboxylic acid examples a "Radical", it's just an alkyl group. A possibility maybe that they consider it a radical since the carbon is donating only one electron to the bond from it's valence shell and that the R group is only donating one as well. So if you treat them seperatley only posessing the electron that is originally theirs, I guess you could refer to them as radicals. But it's a stretch and is pretty misleading. Letting R stand for "Rest" makes a hell of alot more sense. Since that is how it's used. And yeah that OP structure represents a hydrogen bonding formation found in a type of protein secondary structure called an "Anti-paralle Beta sheet", with the R groups represesnting amino acid side chain.

Well first of all this would probably be more appropriate in a chemistry forum even physical chemistry since biochemists don't really deal with this sort of idea. But DNA is a solid. You can't really have it in liquid form without introducing some sort of solvent or mobile phase. It's not possible to heat it up and just melt it as far as I know since it will degrade before it gets hot enough to just melt. However, it is possible to modify it into a special kind of DNA/metallic salt that is molten. http://www.sciencedaily.com/releases/2001/01/010118064934.htm Though it doesn't say in the article supplied I highly doubt that it'd maintain it's double helix structure. It would most likely be in the form of single strands inionically bound to metal complexes.

I'm curious how you'd actually specifically target weeds with electricity, without killing everything else around.

I'm surprised that no one has brought up the speech theory. This is the one I'm most familiar with. The general idea is that panting is an ineffective way of loosing heat for humans since it interferes with speech. How are you supposed to talk properly when you have to pant constantly to loose heat? So the idea is that we lost our hair to allow us to sweat instead to loose heat freeing up our mouths for speech. We all know how impossible it is to talk after running alot and having to breath havily to catch your breath. Now imagine breathing like that all day on a hot day and trying to have a conversation.

Right basically for the recessive defective allels you get from one parent there is a compensating working allele from the other. (And most people get a few defective ones) So if your parents are the same, there is a 1/16 chance for every recessive allelle your grandparents have that you'll recieve a homologus copy of it. Now since the grandparents would be assumed to be a non-inbred that would means on average you'd probably have about 1/16 x (average amount of defective recessive triats per 2 non-inbred people) amount of uncompinsated recessive alleles of "defective" traits given that the average person has a few of these makes those pretty bad odds. now for every generation up that the inbreeding occured there is an exponentially smaller chance of getting a defective recessive trait. The problem really amplifies with very close inbreeding. Well it works like this till you go back close to the average amount of generations back that two non-inbred people share an ancestor, we all share one at some point.

This is believed to have happened through processes that compartmentalised the single celled organism. It is possible for a single cell to be multinucleated so it shouldn't be too hard to imagine a membrane forming between them.