Biochemistry and Molecular Biology
Discussion of protein structure, energetics, and molecular biology.
2095 topics in this forum
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I know this sounds stupid but I only have the basics in biology and microbilogy. It seems to me if the cell can create this germ/disease then why cannot the same cell cure the disease by introducing a destroying agent into the cell and or morphe the negative cell disease into a cancer killing machine to kill all opposing cancer? pljames
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I am currently enrolled in molecular genetics taught by Don Meninger (Harvard graduate) who has worked with scientists such as Messelson, Holliday, and such. This is one of his questions which I thought was a bit confusing at first. He seems to think that the question makes perfect sense. It may be a bit difficult for some of you nevertheless it is a practical problem having to do with practical logic skills which does not require one to be proficient in genetics. After you answer the question, please comment on a scale of 1-5 on how difficult you thought the question was and if there was any ambiguity in how the question was phrased. E coli has a base content o…
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and what do they have to do with genes? are they gene activators? because i came upon an article that had a format similar to this. or could you just decode the meaning of this table. are the things listed (such as Tor2, mTor etc..) genes or kinases? thanks!!!! Table 1. Genes required for the autophagy and Cvt pathways Gene Mammalian homolog Characteristics Induction of autophagy and formation of autophagosome Kinase signaling system Tor2 mTor Rapamycin-sensitive protein kinase APG1 ULK1 SER or THR protein kinase APG6 …
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I'm wondering if anyone knows how N-glycosilation works and why some aminoacids get N-glycolysated and some don't? I'm working with the AA-sequence 421-440 for an isoformof human alpha-amylase, if that is to any help. (shown below) Phe Thr Asn Trp Tyr Asp Asn Gly Ser Asn Gln Val Ala Phe Gly Arg Gly Asn Arg Gly Thank you for any help! /Matilda
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Hey, My blood gp is 'O' and my brothers gp is 'B' and 'AB'. of the basic knowledge of blood gp alleles that I have, we inherit from parents the type of gp that we possess. So accordingly, if I reverse engineer it I find that one of my parents shud hav 'A' and other 'B'. When I enquired i found that my mom is dominant and carries B(hence BB) Thus in that case, with these blood gp's AO x BB | F1 : AB & OB (i.e B) Thus can I conclude that I was one the adopted among all 3 children??? PLease help
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I was just wondering this because I would be a case in point. Neither one of my parents could program a computer if their lives depended on it, but I have an aptitude for computer science and it's what I've earned by degree in. Could it be that a combination of genes leads to unique phenotypes? If this usually doesn't happen, then I must have been adopted!
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Hello Iam working on recombinant fusion protein which has HSP70 as a part of it. (This protein has His-tag too). protein was expressed in bacterial cells and purified using Nickel column under denaturing conditions (8M urea). In order to refold the protein after purification elute fraction (protein eluted with 8M urea pH 4.0) was dialyzed against 10mM Tris (pH 8.0), 0.1% Triton X-100 followed by dialysis in PBS (pH 7.4). Does this procedure refold the protein or not? I need some help in this matter. can anybody answer my question. i appreciate your help very much.
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read topic
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Hi, Iam trying to coat the ELISA with a chemical instead of a protien, and couldn't do it. Can anyone tell how I can coat a chemical onto ELISA plate. Thanks
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Thanks.
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hello I am new to this, and I don't even know if what i m doing now is correct:) erm could I have some help on this exam questionnn plllss thanks alot Protein A was purified using ammonium sulf. precipitation and cation xchange chromatography. The total protein at each step was 500mg, crude extract; 200mg after precipitation; and 10mg after cation xchange. The total activity of Prtotein A was 25 units, crude extract; 15 units, after precipitation; and 7,5 units after cation xchange. How do I determine the %yield, purification factor, and specific activity of protein A at the final step?
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- 5 replies
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ribosomes or RNA? i'm just confused right now.
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- 14 replies
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Hey guys, I know you have probably heard of this questions many times, but is it really possible to clone dinosaurs? What do you think of Dr Schweitzer's discovery of preserved soft tissue in a fossil? Is it real, or does it represent some unknown form of fossilization?
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I know this is a dumb question, but how do you conjugate/combine proteins? The reason I wanna know, is that I need a large quanity of a very expensive antibody for a piece of research I am doing. If I can find out how to conjugate proteins then, I can simply acquire the original substance, conjugate it to a viral protein, and then make a sub-type vaccination, and produce antibodies from that. Could anybody tell me?
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Can anybody solve this problem? I have no idea how to approach this one. Numbers of bacterial in a suspension are usually so large that single colonies would be impossible to observe without suitable dilution. The usual dilutions are 100-fold, in which 0.1 ml of the suspension is mixed with 9.9 ml of dilution buffer; or 10-fold, in which 0.1 ml of suspension is mixed with 0.9 ml of suspension buffer. Usually serial dilutions are necessary, in which the suspension is diluted once into dilution buffer, the resulting suspension mixed thoroughly and diluted a second time, the resulting suspension mixed thoroughly and diluted a third time, and so forth. The serial dilut…
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Hi , I work with a phosphorylcholine containing, tetrameric, N-linked glycoprotein (>200kDa) which is produced in, as close as possible, an endotoxin free environment however when we routinely test it using either a gel clot assay or a chromogenic microplate assay we get very inconsistent results eg adding polymixin to our sample has only a minor effect as does adding glucan blocker. Serial dilution of our sample only has a limited effect. We are presuming that this may have something to do with the structure of our molecule but are at a loss as to what this could be. Has anyone else experienced problems like these or even better has an explanation! Thanks Kitt…
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Hi, This is my first post, I hope of many more to come, but at the moment I'm in need of a bit of help... Basically, I have purified a protein and I wanted to know its yield, but I'm not sure I'm doing the calculations right (its not an enzyme)... Here goes: The initial volume of the Flask in which I made the protein was 2 Litres. The final volume of the cuvette was 600 uL (microlitres). Concentration of Protein in cuvette was (there were 3 samples): 1) 591 uM (micromolar) 2) 456 uM 3) 2141.8 uM The molecular wieght of the protein was 7396.2 (MW). Anyone got any idea about how to go about calculating the yield? I worked out the molar…
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Hi all, I know this might not make sense, but can any one explain?? we know that plants grow faster and bigger in darker position that in light position, because of etiolation.... but my experiment of investigating phototropism in contradiction of geotropism surprised me.... I have 3 plants on the shelf of a dark chamber, the distances between each 2 plants are 60 and 30 cm away repectively. just beneath the middle plant, I place a torch, which is situated abit outwards rather than light directly on the middle plant.... For days of experiment I saw 1 thing, the plant at the left most, where received the slightest light, barely grow, and the plant at th…
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It is said that a virus can not attach nother virus due to protien protien interaction between the "walls" of the viruses. so it is possible to give immunity to a cell against any virus by simply adding the protien seqence from the caspid of the virus wall to the cell wall of the cell. so now that the cell has the protien on its wall the attacking virus will 'think; the cell to be another virus and hence will not attack it. can this whole strategy be developed for complete systems instead of just one cell
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Hello Everybody, I am going to subgroup GH (Growth hormone releasing) pituitary adenomas according to their expression profiles by microarray and RT-qPCR. I do have 50 GH pituitary adenomas to subgroup and i wonder should i run all these 50 adenomas in the microarray to check their expression profiles or should i only take for example 5 of them to run in the microarray since they probably must have almost the same expression profiles? You know if i run all the 50 adenomas then it would take alot of time. What do you usually do when you have to subgroup a group of related things like in this case GH (Growth hormone releasing) pituitary adenomas? Thanks for an…
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The technique involves using proteins called zinc finger nucleases to bind to a specific sequence of DNA, which contains a harmful mutation, and then cut both strands. The cells own DNA repair mechanisms are stimulated into action by the broken double-stranded DNA. A piece of DNA containing the correct sequence is also inserted into the cell, which acts as the blueprint for the repair mechanisms to produce the desired sequence. The technique has now been performed on human cells with some success. It is hoped that it may prove useful for people suffering severe genetic diseases, and that it will have fewer side effects than existing methods. From: http://www.newsc…
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It was recently published in March edition's Scientific American. It seems that one gene can infact code for many many proteins, (sometimes up to 6+), this is mainly due to a different perspective on gene expression. Where introns are infact quite important after all, even though they are not "expressed" they play a crucial role in gene expression and protein synthesis. But what are the factors that tell genes to code one protein and not the other? I'm guessing environmental and the body's regulatory mechanisms as of right now. (anyways, i'm a bio-chem newb , if anyone can add/explain more to it it'd be great)
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Hi I was wondering if someone knows any good electronic resource (or book) about enzyme kinetics, specially trouble-shooting. I know it is simple, but I am stuck just trying to measure the concentration of a substrate I am working with using a coupled enzyme assay. It is supposed to be very straightforward, but I am getting pretty weird results. Any help would be really appreciated.
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Hi all, I can't seem to find any diagrams on the web showing the flow of electrons for the mechanisms for the N4 methylation of cytosine, N6 methylation of adenine, and 2'O methylation of ribose. I checked my biochem and molecular bio book, but neither of them have them. Any help is appreciated. -Steve
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I'm interested in learning as much about biochem as I can get my hands on. Although this is an EXCELLENT site for information, it is located is disparate posts. I'm wondering if there is a general overall biochemistry site or post or pdf that I can download and read? Possibly for other subjects as well (math, physics, etc.). Thanks a bunch. -Stephen
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