Biochemistry and Molecular Biology

Hi, I was wondering if anyone has any knowledge about Focal Adhesion Kinase (protein tyrosine kinase 2). I am doing a basic report on it, that needs information on 1. Where it is found, 2. Its structure, 3. Its Mechanism of Action, and 4. Role of enzyme in human disease/therapy. I mainly need guidance to 1. and 3 if anyone has any sites or papers that would be appreciated. I did some research myself and found alot of cancer research and the role of this enzyme, but I cannot seem to find where it is found (surprisingly), but I am assuming Focal Adhesion is located in the cytoskeleton, while the protein kinase complex is found in the extracellular matrix (But I do not know …

Hello, I have a module called Metabolism which is basically biochemistry and I'm struggling to find a book or particular thing that could help me with the basic understanding. The module topics are things like: biomolecules thermodynamics - catabolism and anabolism glycolysis/ gluconeogenesis/ glycogen oxidative phosphorylation proteins and amino acids fatty acids, lipids and membranes all my books are sort of vague and i don't want to buy a biochemistry book and have to revise the whole thing for one module. can anyone suggest any books that might help with basic understanding before i revise it in further detail. thanks.

Hi, <br style="color: rgb(40, 40, 40); font-family: helvetica, arial, sans-serif; font-size: 14px; line-height: 22px; "><br style="color: rgb(40, 40, 40); font-family: helvetica, arial, sans-serif; font-size: 14px; line-height: 22px; ">i know that blood glucose level can be directly measured using the Glucometer. but I would like to know the biochemical methods to measure the blood glucose level. .<br style="color: rgb(40, 40, 40); font-family: helvetica, arial, sans-serif; font-size: 14px; line-height: 22px; "><br style="color: rgb(40, 40, 40); font-family: helvetica, arial, sans-serif; font-size: 14px; line-height: 22px; ">Can any one help me !&l…

Hello everyone! I'm a beginer in modelling proteins. I did some predictions in the Modeller and did the validation, but I don't know if the data that I got are good. Someone know a paper that discusses about good values to ramachandran, RMSD and others parameters?

At work we use Tryptic Soy Broth media for detection of microbiological contamination. We have had more than one instance where no contamination was detected; however, the broth was observed to have fiber-like particles or formations present which were identified as protein. Prior to use, the broth is filtered. Does anyone have any idea of how/why these fibrous protein formations are occuring?

What method is used to isolate (and culture) stems cells removed from a blastocyst? would that method be different if you were tasked with isolating stem cells from an apple seed? Thank you in advance for discussion :]

Hi all! Does alcohol cause blood cell agglutination? Or agglutination in alcohol abuse possible in very high (lethal) promille dosage (50-100 promille)? Death - about 7 promille.

When forming the following equation to determine the rate of enzyme activity what is the mg of protein? Product Produced in mmol/time (min/sec etc)/mg of protein Is it the amount of substrate used? The sample? for example the amount of bacterial cells, though I'm not sure how you would determine its mass. Usually when they refer to protein they mean the enzyme, but I do know that enzymes usually cannot be quantified in terms of mass? Anyone know?

Does every person, infectious and healthy have levels of IgM in their blood? I ask because i recently had blood work done in relevance to thinking i have HIV, my tests were negative for p24 and anti hiv, however, my IgM level was low and my plat count was low thx

Why did the trees not rot during the carboniferous period? I heard on an "Eden planet earth type program" that as plants moved on to land, fungihad not evolved to break down the cells yet and it took them hundreds ofmillions of years to work it out. Am I correct toassume; that the reason we have an abundance of coal reserves is due to; there being nobiological mechanism (in the form of bacteria or fungi )during the Carboniferous period, to decompose the “ vastswathes of forest that covered the land, which would be laid down andeventually become the coal beds” Any Ideas? Thanks Brian 911

Hey everyone, I'm trying to see if I can get C. elegans to eat pure hydrolyzed Casein (protein found in cow's milk) in liquid media. Does anyone have any suggestions as to approximately how much casein I should put in the media (S-Medium) if I have about 10 worms per well? Thanks!

Can someone explain as to how the entrance counerflow assay works and the principle behind it..

I am trying to understand the function and purpose of some of the parts of a plasmid. Could someone please explain the following terms: Long Terminal Repeats 5' and 3' UTR (untranslatable regions) left and right homology arms

I have got a question relating the DNA replication forks and I have been unable to find out the answer from my books. I am new to molecular biology only started it about two weeks ago. I know and understand the idea of the DNA replication happening in the replication forks. So if we presume that the replication fork goes into left side with the top strand being the leading str and the bottom the lagging it makes all sense to me. But its says in the book that the replication forks are bidirectional so it can go to right hand side at the same time. So does that mean that if it goes to right side the top strand become the lagging strand while the bottom becomes the lead…

Hi I'm new here so I hope that this is in the right place. So I have been considering heterologous expression systems, particularly for expressing proteins, and I was wondering what people considered are the main advantages and disadvantages of their use? I could think of a few, but wondered if there were others? As far as I can tell the over-expression of the protein can be both advantageous (as it is easy to measure effects) and disadvantageous (may force interactions that would not normally occur, like oligomerisation of receptors). Other advantages are that they are easy to grow and manipulate genetically. But they are devoid of key interacting proteins an…

Hi Everyone, I've been trying to develop a chloride-sensitive assay for an ion channel protein using a liposome system. The problem is that the equilibrium is shifted towards the free protein in solution rather than bound to the liposome. Are there any methods/conditions that I could use to improve the amount of protein bound to the liposome? I'm currently using a 4:1:1 ratio of PC:PS:cholesterol for the liposomes prepared by extrusion and freeze-thaw Thanks

Hi, Just having an issue with making up a solution and don't trust myself that i am doing it properly! My protocol says that i need to prepare 0.05M Tris HCL buffer PH 7.4, containing 1.0M NACL, 20mM EDTA, 1mM PMSF. I need to make 3ml in total. I have 1M stock solution of Tris HCL buffer PH 7.4, and EDTA, NACL, and PMSF in solid form. I am thinking that I probably do not need the NACL as its purpose was probably to adjust the PH to the desired level but as mine is already at 7.4 i might not need it. Does anybody know the right quantities to make up this solution or can offer any advice in this area i would greatly appreciate it. Thanks Siobhan

Hi ! I am working with isolation of plant histone proteins. 1) Currently I am using acid extraction method to isolate histones from 10 g of leaves. 2) Bradford protein measurement to measure protein concentration in isolated samples, so that i can load desired amount of protein when I use western blotting. Problem is: when I run all the Histone samples on a gel to perform western blot, protein bands migrate at different pace and stop at different positions(first band at ~15 KD, second and third protein band ~20 ). even though all the bands contain same sample Why I worry so much because I use specific antibody, they should be located at one part…

Hi what's the difference between ligands and cofactors and what are the differences (if any) in their role of allosteric enzyme regulation/modulation?

Hello. We are going to buy a microscope for live cell imaging. Now, after some months of discussion, we end up with two brends - NIKON and Leica. Does anybody worked with this microscopes? Which brend you would suggest for live cells imaging?

Hey, I have previously knocked out a gene of interest in pseudomonas putida, and replaced it with a gentamicin cassette. Surrounding the gent gene are FRT sites. This part seemed to work fine, the mutants grow on gent, while the wild type do not. However, now I am trying to electroporate a plasmid containing FLP into these mutants so that FLP can remove the gent resulting in unmarked mutants. On the FLP plasmid I have (pFLP2) is a beta-lactamase gene... however, when I electroporate into the mutants and select with carbenicillin, I get equal background growth (a full on smear) on the control plate (electroporated with no pFLP2) as on the pFLP2 electroporation plate. P. …

Good evening, I am currently a first year molecular biology student at university. I just have a question and I hope that it's okay to ask here. I currently have a simple expression system setup within E.Coli K12 strains, using a phagemid with Tet-R/Amp-R genes, and my gene of interest inserted downstream of the T7 promoter however there is no T7 terminator present as far as I know. I plan to introduce a heat-inducible plasmid containing the gene for the T7 RNA polymerase under the control of an E.Coli promoter into the cells, and induce it in the presence of labelled amino acids, and Rifampicin to inhibit endogenous RNA polymerases in the hope of translating primaril…

Hi, I'm reading a couple of papers about making transducible proteins (proteins that can pass through the cell membrane) and it seems the way to do this is to make a fusion by attaching a protein transduction domain (PTD) onto whatever protein your interested in making transducible. Now it seems this is done by cloning the gene(s) needed to make your protein of interest into a plasmid that already contains a PTD. I'm just wondering how the PTD plasmid is made in the first place. It seems like what you have to do is somewhere in between your promoter site and your multiple cloning site you have to insert a 6 histidine sequence, followed by your PTD sequence, and then a gly…

On several ocations I've stumbled upon explanations like "Photosystems in plant ancestors evolved in a different environment and now it's sort of "stuck" the way it is, it's too hard to change it", "The plant would become too hot!", and "The plants can't handle so much energy". I am a bit skeptical about these explanations, but if you have any data testing any of these hypothesis I'd love to know about it. While reading "Photobiology: The Science of Life and Light" (Amazing book) I stumbled upon what looks like an explanation. The problem is that I can't fully understand it, and I would like your help. You can read it here: http://books.google.com.mx/books?id=bRW…

Dear, I have been given a topic to find out the "Effects of different containers on the Microbiological Quality of Bottled and Fresh water". Can you guide me and tell me what are the microbial parameters that i need to consider while finding the effects of containers, Also tell me, how do we perform the Heterotrophic Plate count and APC count on the water, can you give me the link to some papers for this?, i would like to know different materials and method required to find to run the HPC count in the water Waiting for your Kind reply.. Regards Basra