are syntetic proteins bad for liber?
473473
yes and no.\nyou should not take too many, and drink a lot of water to take the strain off your liver and kidneys.\ntoo much protein in any form can upset your stomach. arginie, an amino acid found in many proteins can cause weakness, nausea and diarrhea in excess.\nyour body has evolved to process proteins. there shouldn't be much difference between synthetic and natural.
819615
Hydrochloric acid has several functions during digestion.  Gastric acid has a pH of around 2.0, which is highly acidic.  Since proteins have a narrow pH threshhold, gastric acid denatures them and exposes peptide bonds for proteolysis.  \n\nThe real work of breaking the peptide bonds is done by pepsin though.  However, since pepsin targets proteins and there are many proteins in body that we don't want pepsin to break up, pepsin has to be produced and transported around in the form of it's inactive precursor, pepsinogen.  Once the pepsinogen encounters the HCl in the stomach, it is activated into pepsin and proteolysis can occur.  \n\nStomach acid is also useful in killing any bacteria that have entered the stomach through the esophagus and keeping the beneficial bacteria in the colon from migrating into the small intestine and causing problems.
348364
Too many simple carbs. Go with more protein & more complex carbs, while avoiding simple carbs.
828553
At physiological pH most of the -COOH of amino acids are deprotonated (-COO-) and -NH2 protonated (-NH3+).\nIf you increase the pH then the -COO- will remain as such but the -NH3+ will lose the proton. -NH3+ can act only as an H-donor for an H-bond so such a bond will be broken. However if the geometry and number of interacting partners allow it it could be replaced by another H of the same -NH2 group.\n\nTyrosine has pKa around 10, so if you go to extremely basic pH it will be deprotonated and thus it will not be able to act anymore as an H-donor for a hydrogen bond and the bond will break. If however it was acting as a lone pair donor, the bond will become even stronger.\n\nGenerally when the pH change (extremely basic or acidic) causes changes in the charge of the group can but not necessarily breaks H-bonds. An important note: even if the H-bonds are not completely broken there will be rearrangement (some bonds might break and others form as the some H-donors become H-acceptors and vice versa) changing the conformation/folding of the protein.\n\nFor sure the effect of pH on ionic bonds is far greater than that on H-bonds.
860270
Hi - here are some ideas without seeing your actual data.  First - the system was too hot during transfer to  the membrane - be sure you aren't running it at too high  a voltage.   Second, not an issue with the  blot,  but with  the gel  - was it expired?  not fully polymerized? were the  wells free of debris when loading  samples?   sometimes with highly concentrated samples, especially cell lysates,  this  can  happen  because  of  viscosity  in t he  sample  (from  DNA for example). good  luck.
1137440
True!! If you don't eat proteins then your body won't receive things that your body needs in order to develop! Your body won't  develop and you'll have serious illness that can affect you bad! That's why I encouareg you to eat as much proteins as your body needs. Just like we buyt thing we need in order to survive, our body also needs proteins in order to continue running like a car does!
335320
Trypsin cleaves c side of arg and lys so this fragment is probably the c terminus
810190
No, soy protein is bad for you.  Read these articles:\nhttp://www.mercola.com/article/soy/index.htm
513695
That is because heat destroys the structure of a functional protein.\nproteins are long chains of amino acids. This chain of amino acid folds up into a 3 dimensional structure via intramolecular forces. like you can fold up a long, blown-up balloon into a giraffe or a dog. With this structure, proteins are able to perform its functions. but when you heat the protein, you break the bonds in the amino acid chain, unfolding it and destroying its 3 dimensional structure. (IE, breaking the giraffe back to a long baloon, obviously it doesn't look like a giraffe anymore) and the protein cannot perform its functions.
416140
Lysogeny broth (LB), a nutritionally rich medium, is primarily used for the growth of bacteria. It is also known as Luria broth or Luria-Bertani broth.\n\nLB media formulations have been an industry standard for the cultivation of Escherichia coli as far back as the 1950s. These media have been widely used in molecular microbiology applications for the preparation of plasmid DNA and recombinant proteins. It continues to be one of the most common media used for maintaining and cultivating recombinant strains of Escherichia coli.\n\nThere are several common formulations of LB. Although they are different, they generally share a somewhat similar composition of ingredients used to promote growth, including the following:\n\nPeptides and casein peptones \nVitamins (including B vitamins) \nTrace elements (e.g. nitrogen, carbon, sulfur) \nMinerals \nPeptides and peptones are provided by tryptone. Vitamins and certain trace elements are provided by yeast extract. Sodium ions for transport and osmotic balance are provided by sodium chloride. Bacto-tryptone is used to provide essential amino acids to the growing bacteria, while the bacto-yeast extract is used to provide a plethora of organic compounds needed for bacterial growth
431813
Tag it with a poly ubiquitin chain.  You can make a chimera of the protein plus a couple of ubiquitins.  We did this for our protein (one ubiquitin tag at C terminus) and found it was degraded very efficiently.
798909
Protien shakes, vitamins, and teas
653429
Yes proteins are amphoteric, they do contain both acidic and basic residues, but the charge on the protein is dependent on the degree of dissociation of the acidic or basic groups. \n\nThe Tris-HCl buffer used in gel electrophoresis(assuming you are talking about PAGE, most commonly used for proteins) has a pH of 8.7. At this pH the protein molecules have a net negative charge, hence they move towards the positive electrode. Their difference in mass leads to their separation as does the amount o charge that they carry.\n\nIsoelectric focusing uses the amphoteric nature of proteins to the max - it uses the isoelectric point of the protein for its separation. The isoelectric point is the pH at which the protein has no charge and hence it stops moving in the electric field.
604378
Are you talking about Bromelain? It is not toxic except at high doses but I would be very careful about taking it . I would check with a licensed Physician because it may interact with other drugs.\n\nYou might also check with a licensed Naturopathic Doctor. \nBromelain is measured in GDU or gelatin digesting units. It essentially breaks down proteins. It would never be a good idea to act solely on the basis of advice received over the internet.\n\nYou can do a google search to find articles about Bromelain.
399837
No, the protein is broken down in stomach, absorbed in the small intestine, and the remainder is expelled.
565059
syninol fluids around joint is not flowing freely
1153019
L-Tryptophan is better than 5HTP\n\nhttp://www.papanature.com/store/ProductsList.aspx?c=Herbs&cid=l_tryptophan&gclid=CPHUxZLbx4UCFQ8fSgodigIitg