Biochemistry and Molecular Biology

Can someone please help me answer this question? Thanks!!! 4.5 mL of a protein with concentration 48.2 microM is placed inside a dialysis membrane, which is then placed inside a beaker containing one liter of 20 mM HEPES buffer at pH 7.5, plus 14.5 microM of a fluorescent ligand. The dialysis membrane permits the ligand to pass through but not the protein. The solutions are allowed to set over night to reach eqilibrium. After equilibrium is reached, fluorescence measurements are used to establish that the total ligand concentration inside the membrane is 62.7 microM, and the total ligand concentration outisde the membrane is 13.5 microM. The protein concentration insi…

How does multiple sclerosis lead to kidney failure?

Hi I'm intending to run an experiment involving bacterial colonies on agar plates. Unfortunately I do not have access to a fume cabinet or sterile room to keep them in. Are there any alternatives to using a fume cabinet? or does anyone know of any websites or companies that sell good, cheapish secondhand laboratory equipment? Thanks Iain, a uk based lab technician

Hi guys I'm really stuck right now and I hope someone can help me. I just began my master thesis and I have to prepare an experiment. We would like to produce small unilamellar vesicles (SUVs) and insert a dehydrogenase (retinol dehydrogenase, RDH5) into them, since its a membrane protein. Could anyone tell me, how this could be done? I know how to prepare SUVs (read some papers about this procedure) but I don't really know, how to insert the dehydrogenase constructs ?! Perhaps express them in E.coli first and then mix them somehow with the SUVs? I hope someone can help me Cheers, dafenris

Under the microscope there's a protein in the membrane... How will I know weather this protein has been on the membrane since it delivery or has been recycle to the cell and back to the membrane ??? I hope to found an answer ^^ All My Regards JOJO

I just wonder why beta sheets are always twisted. Thanks!

If someone autoclaved a lysis solution with the lysozyme in it, would the lysozyme denature?

I read in this article that nine cats survived to temperatures as low as 12,5 through hypercapnia and hypoxia. I understand that this reduces oxidative stress, which can no longer be controlled by the body when it's chemical activity has been so far reduced, to an absolute minimum, but doesn't the body spontaneously break down through its entropy? Or is the entropy so reduced along with the temperature that it is no longer very significant? Aren't there reactions needed to keep the tissues from falling apart by themselves? I have the feeling I'm overlooking something. I'm not sure how long the cats survived at this temperature, though of course it can't have been very lon…

Now, this being said you would have to be either insane or just really mentally challenged to do this.. but here is my theory and my question.. of would this be possible to create a Armageddon virus? It is a common myth and story in most horror movies that a flesh eating monster re-animates after death and then roams to kill more and then transmit the virus to others... these monsters are known as Zombies. While fake in most part - with scientific breakthroughs and such that we have now it brings to life the question of if this could truly happen? Now to get myself straight I'm not saying creating a new virus from nothing. But I am saying that what if I (in theo…

I will like any protègè, 2 ellucidate on synthesis of protein by artificial means.Is it posible?

Dear all, I am in need of lecture notes on "Biochemistry and toxicity of metals". Pls help to find that... Or does any one have article on that topic.. Pls help me!!! Thanks

Many believe this relatively simple inexpensive compound is very effective in treating such troublesome and deadly viruses as hepatitis-C,herpes I and II, AIDS, and on and on. It`s antiviral properties have been discussed at least since Person,Snipes,Kieth and Cupp`s article: BHT INACTIVATES LIPID COATED VIRUSES back in the 1970`s. Much has been written since then on this subject.Speculation is that these bulky hydrophobic molecules are drawn to and disrupt outer lipid containing coatings on many viruses thereby destroying them. ...DS

Hi everyone, I am looking for a book that will be a good second resource (other than the textbook) for me while I make my way through my first Biochemistry college course. I'm thinking something along the lines of "Biochemistry for Dummies". I see that there is actually a book called "Biochemistry for Dummies", but I am wondering if that is my best bet, or if there is something even better out there. Something that is a good overview of Biochemistry that will give me an extra advantage for scoring high on the course exams. I would appreciate ANY insight you can give me. Thank you very much! -Mandy

How would I regenerate an HPLC column after it has *dried out? * Dried out means, someone else took my column off the HPLC machine for me and didn't replace one of the end fixtures. I didn't realize this until ~2.5 weeks later. Air hasn't been pumped through the column, but I'm getting unusual UV traces (High absorbance in irreproducible areas). Does anyone have any suggestions?

What happens during the process of conjugating BSA to oligos and BSA to SANH? In other words, what is the science behind it? Okay, so I'm doing a research report. I followed a protocol for the modification of BSA. I want to see if conjugating BSA to oligos will increase the sensitivity of the results in my DNA microarray chip. So far, I conjugated BSA to oligos powder and also conjugated BSA to SANH. After running a protein gel, I saw that the well that BSA conjugated to the oligos shifted upwards compared to the well that had BSA conjugated to SANH. Therefore, I can see that the oligos and the BSA did bind. Hopefully, this will increase the sensitivity of my r…

I wanted to do some stains but i dont know where to track down some dyes. Can you make them at home or do you have to buy them? Was thinking if i could use food dye but i dunno.

I was thinking of making some basic amino acids recently, to try some basic dry- heat, protein synthesis. I've been playing around with some basic chemicals I have on hand, but I can't really find a way, to keep the amine and the carboxyl group, from reacting with one another. Any thoughts or ideas? At this point, I'm rather clueless. As always, help is most appreciated.

I want to mutate the residue Glutamate or Arginine in a protein so as to break the saltbridge between them . Can any body suggest a residue to replace lets say Glutamate inorder to break the salt bridge? So far I am considering Glutamine in place of Glutamate. Gaurav Bhatti

I need to make a series of 6M and 8M guanidinium HCl buffers for a protein purification, but I can't seem to get the GdnHCl into solution. I'm able to make a clear 8M solution, but when I make the 6M solution, theres some sort of cloudy precipitate that eventually settles. I've tried using the 8M solution as a stock and diluting it down to 6M, but I've noticed that it starts to crash out at around 7.3M. Heating it to 35C doesn't make a difference, nor does stirring it for several days. Is there some trick to it or has my GdnHCL probably gone bad?

Hello, I'm trying to convert a kcat/km obtained from a journal article from s-1*uM-1 to s-1*M-1. kcat = .55 s-1 Km = 71.7 uM kcat/km = .008 s-1*M-1 I'm assuming that I just need to convert the 71.7 uM into M (.0000717M) and then divide to get the value 7670 s-1*M-1 However, and older, much respected labmate claims the value should be 4.8 E5 in his notes. Am I doing my math wrong? Thanks!!! Merged post follows: Consecutive posts mergedI turns out they were converting it to min-1 * M-1 not s-1* M-1. Thanks!!

i am humbly asking anyone who can help me access pdf journals that has somethig to do with peripheral blood micronucleus assay. I am about to do research. I will be screening the antimutagenicity of Garcinia mangostana or mangosteen. methods on determining MTD or maximum tolerated dose and on acridine orange staining will also help a lot.

Sorry if this is in the wrong section, I am new to hear and do not know much about science. I would appreciate as much help as possible and for you to treat me like an idiot in your explanations please. My problem: When you cook potatoes by boiling them, they take a while, i presume it is something to do with the break down of the proteins or something like that? I am just wondering is there a scientific process you can do to speed up this reaction? Sorry i have not explained very well and if any one needs any more infomation or a better explanation to give me answers then please state and i will try and explain in more detail. Thanks very much for all your help in advanc…

Hi, I was lately trying to do a rescue of a gene knock out I did in yeast. I got a good phenotype from the knockout but could not restore the knockout by cloning the gene back in. Now I am trying to figure out why. Originally I cloned my gene into a yeast vector which uses a uracil marker, but was instructed to remove the uracil marker from my knock out first since it already had that one. So I cultured the yeast in medium with 5'-floroorotic acid which selects against ura3 producing cells. This was supposed to remove the marker, so I cultured the colonies in rich media and then did a transformation using the LiAc method. At that point I believed I had my knock out wi…

Phase 3 studies being conducted by Harvard Medical school on this medication. We all know it increased the life span of Mice by 30 %. Due to the fact that this can be obtained by food supplement such as Red wine, there are many Vitamin suppliers that distribute this medication already. Drinking Red wine is Not advisable due to the fact that you have to drink massive amounts. Many Vitamin companies have doses up to 300-2000mg pills. FDA is not regulating this at the moment. There are some reports of side effects such as Joint pain, dry skin etc. I am in healthcare myself and am a believer. Preliminary reports from Harvard medical school looks really good so f…

Hi, I am currently working in a lab for the summer and the professor I have been working with wants to perform a 2D gel electrophoresis on rat brains. As an undergraduate, he has asked me to look up a procedure to perform 2d on rat brains which will assist him later on in his experiments, while it will help me get a good grade for coop/recommedation. I did find a procedure to homogenize rat brains but I am unsure of the amounts to use. I plan to use 0.01g of rat brain but in the article it says : Homogenization was performed in (Sol B) was: 7 M urea, 2 M thiourea, 40 mM Tris, 3 mM tributylphosphine,2% CHAPS, 1% Pharmalytes 3.5–10. How does one figure out how much to use f…