how Amino acids are processed into urea?
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The Amino group (NH2) breaks off the amino acid molecule by a process called deamination and forms ammonia. Toxic ammonia is rapidly converted to urea by a process called the ornithine cycle.\nUrea is only slightly toxic.
1061977
(H+) + NH3 -> NH4+\n It makes an ammonium ion, if you are talking about a hydrogen ion and not H2.
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Yes,amino acids are healthy. Amino acids make up proteins, and proteins are essential to build muscle tissue. You can get all of your amino acids from meat, fish, and cheese. Legumes, such as beans and lentils, have incomplete amino acids, so to complete them, just add nuts and seeds.
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carboxly and amine groups.\n\nCheck out, http://en.wikipedia.org/wiki/Amino_acid for more info about amino acids and what the structure looks like.
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a) carboxyl and amine groups\n\nan amino acid is any molecule that contains both amine and carboxyl functional groups
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transamination is involved in the interconversion of certain amino acids. \nEg Aspartate Aminotransferase catalyzes the movement of an amine group from glutamine onto α-ketoglutarate.\npyrodoxal phospate is a co factor of many of these enzymes including Aspartate Aminotransferase.
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In biochemistry, denaturation is a structural change in biomolecules such as nucleic acids and proteins, such that they are no longer in their native state, and their shape which allows for optimal activity.\n\nThis change is usually caused by heat, acids, bases, detergents, alcohols, heavy metal salts, reducing agents or certain chemicals such as urea.\n\nContents [hide]\n1 Protein denaturation \n1.1 How denaturation occurs at levels of protein structure \n1.2 Loss of function \n1.3 Reversibility and irreversibility \n1.4 Some common examples \n2 Nucleic acid denaturation \n \n\n\n[edit]\nProtein denaturation\nProteins denature when they lose their three-dimensional structure - their chemical conformation and thus their characteristic folded structure. Proteins may be denatured at the secondary, tertiary and quaternary structural levels, but not at the primary structural level.\n\nProteins are long strands of amino acids linked together in specific sequences. A protein is created by ribosomes that "read" codons in the gene and assemble the requisite amino acid combination from the genetic instruction, in a process known as translation. The newly created protein strand then undergoes post-translational modification in which additional atoms or molecules are added, for example copper, zinc, iron. Once this post-translational modification process has been completed, the protein begins to fold (spontaneously, and sometimes with enzymatic assistance), curling up on itself so that hydrophobic elements of the protein are buried deep inside the structure and hydrophilic elements end up on the outside. The final shape of a protein determines how it interacts with its environment. If the shape of the protein is altered through some form of external stress (for example, by applying heat, acid or alkali) then it will no longer be able to carry out its cellular function. This is called denaturation of the protein.\n\nDenatured proteins can exhibit a wide range of characteristics, from loss of solubility to communal aggregation.\n\n[edit]\nHow denaturation occurs at levels of protein structure\nIn quaternary structure denaturation, protein sub-units are dissociated and/or the spatial arrangement of protein subunits is disrupted. \nTertiary structure denaturation involves the disruption of: \nCovalent interactions between amino acid side chains (such as disulfide bridges between cysteine groups) \nNoncovalent dipole-dipole interactions between polar amino acid side chains (and the surrounding solvent) \nVan der Waals (induced dipole) interactions between nonpolar amino acid side chains. \nIn secondary structure denaturation, proteins lose all regular repeating patterns such as alpha-helices and beta-pleated sheets, and adopt a random coil configuration. \nPrimary structure, such as the sequence of amino acids held together by covalent peptide bonds, is not disrupted by denaturation. \n[edit]\nLoss of function\nMost biological proteins lose their biological function when denatured, For example, enzymes lose their catalytic activity, because the substrates can no longer bind to the active site, and because amino acid residues involved in stabilizing substrates' transition states are no longer positioned to be able to do so.\n\n[edit]\nReversibility and irreversibility\nIn many proteins (unlike egg whites), denaturation is reversible (the proteins can regain their native state when the denaturing influence is removed). This was important historically, as it led to the notion that all the information needed for proteins to assume their native state was encoded in the primary structure of the protein, and hence in the DNA that codes for the protein.\n\n[edit]\nSome common examples\nWhen food is cooked, some of its proteins become denatured. This is why boiled eggs become hard and cooked meat becomes firm.\n\nA classic example of denaturing in proteins comes from egg whites, which are largely egg albumins in water. Fresh from the eg
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Amino acids are the basic structural building units of proteins. They form short polymer chains called peptides or polypeptides which in turn form structures called proteins. The process of such formation from an mRNA template is known as translation, which is part of protein synthesis.\nPhenylalanine is one of the standard amino acids.\nEnlarge\nPhenylalanine is one of the standard amino acids.\n\nTwenty amino acids are encoded by the standard genetic code and are called proteinogenic or standard amino acids. Combinations of these amino acids produce every single essential protein for the homeostasis of the human body. At least two others are also coded by DNA in a non-standard manner as follows:\n\n    * Selenocysteine is incorporated into some proteins at a UGA codon, which is normally a stop codon.\n    * Pyrrolysine is used by some methanogens in enzymes that they use to produce methane. It is coded for similarly to selenocysteine but with the codon UAG instead.\n\nOther amino acids contained in proteins are usually formed by post-translational modification, which is modification after translation in protein synthesis. These modifications are often essential for the function of the protein.\n\nProline is the only proteinogenic amino acid whose side group cyclizes onto the backbone: it links to the α-amino group, and thus is also the only proteinogenic amino acid containing a secondary amine at this position. Proline has sometimes been termed an imino acid, but this is not correct by current nomenclature rules.\n\nOver one hundred amino acids have been found in nature. Some of these have been detected in meteorites, especially in a type known as carbonaceous chondrites. Microorganisms and plants can produce uncommon amino acids, which can be found in peptidic antibiotics (e.g., nisin or alamethicin). Lanthionine is a sulfide-bridged alanine dimer which is found together with unsaturated amino acids in lantibiotics (antibiotic peptides of microbial origin). 1-Aminocyclopropane-1-carboxylic acid (ACC) is a small disubstituted cyclic amino acid and a key intermediate in the production of the plant hormone ethylene.\n\nIn addition to protein synthesis, amino acids have other biologically-important roles. Glycine and glutamate are neurotransmitters as well as standard amino acids in proteins. Many amino acids are used to synthesize other molecules, for example:\n\n    * tryptophan is a precursor of the neurotransmitter serotonin\n    * glycine is one of the reactants in the synthesis of porphyrins such as heme.\n\nNumerous non-standard amino acids are also biologically-important: Gamma-aminobutyric acid is another neurotransmitter, carnitine is used in lipid transport within a cell, ornithine, citrulline, homocysteine, hydroxyproline, hydroxylysine, and sarcosine.\n\nSome of the 20 standard amino acids are called essential amino acids because they cannot be synthesized by the body from other compounds through chemical reactions, but instead must be taken in with food. In humans, the essential amino acids are lysine, leucine, isoleucine, methionine, phenylalanine, threonine, tryptophan, valine. Histidine and arginine are generally considered essential only in children, because of their inability to synthesise them given their undeveloped metabolisms.\n\nThe phrase "branched-chain amino acids" is sometimes used to refer to the aliphatic amino acids: leucine, isoleucine and valine.
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proteins are broken down to short chains of polypeptide in the stomach, which only takes about an hour after the protein is consumed.\n\nshort polypeptides are then broken down to amino acids in the small intestine. so the entire process should take no more than sevreal hours to complete.
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click on this link http://www.tiem.utk.edu/~gross/bioed/webmodules/aminoacid.htm and look through the table. the answer should be there.
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l-glutamine is an amino acid. the human body 'builds' l-glutamine. it is made of valine and isloleucine. you can buy l-glutamine as a food supplement when doing a lot of sports. it is used during itense training excercises (you do not have to additionally take it when not lifting weights like crazy,...)\n\ngood luck
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What an odd question! This is actually curiosity and not just someone posting their homework!\n\nThe answer is that this won't happen. You have to eat all the essential amino acids before protein synthesis can even begin. This is not a problem unless you are a vegetarian (most plants don't contain all the essentials). Because it won't even start unless there are enough amino acids to finish the job, it won't start then stop. If there is an insufficient supply of amino acids, your body will actually digest your own muscles before starting something that it can't finish.\n\nWhat would happen if you tricked your body into thinking it was well-supplied? I don't know, but it would make a great thesis paper! I'm pretty sure no one has ever found a way to do this.
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urea is a waste product that is excreted in sweat to eliminate it from the body
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You will still have to read the info at the links below as it is "assumed that you have a rudimentary understanding of basic concepts of protein and nucleic acid structure, as well as enzyme kinetics and mechanisms."\n\nI digress to say that "amino acids are the principal building blocks of proteins and enzymes. They are incorporated into proteins by transfer RNA according to the genetic code while messenger RNA is being decoded by ribosomes. During and after the final assembly of a protein, the amino acid content dictates the spatial and biochemical properties of the protein or enzyme."\n\n"The amino acid backbone determines the primary sequence of a protein, but the nature of the side chains determines the protein's properties. Amino acid side chains can be polar, non-polar, or practically neutral. Polar side chains tend to be present on the surface of a protein where they can interact with the aqueous environment found in cells. On the other hand, non-polar amino acids tend to reside within the center of the protein where they can interact with similar non-polar neighbors. This can create a hydrophobic region within an enzyme where chemical reactions can be conducted in a non-polar atmosphere. Likewise, enzymes can also have polar amino acid substituents within the active site that provide a polar region in which to conduct biochemical synthesis."\n\n\n1. Structure of Amino Acids\n2. Review: Basic Concepts of Protein Structure\n3. The Basics & Definitions
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Anabolism is the part of metabolism that refers to building of molecules, therefore, it would seem reasonable to anser there strangely worded questions thusly:\n\n1) since Amino Acids are used to build proteins and peptides, anabolism of amino acids yields proteins and peptides;\n\n2) since glucose is used to build glycogen, anabolism of glucoos will yield glycogen.\n\nGood luck!
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Protein synthesis is not the simplest process, but I will try to keep this answer as simple as possible.  Here I present a highly simplified reduction of the process of protein synthesis.\n\nmRNA made in the nucleus of a cell is transported to the cytoplasm of a cell.  When mRNA is in the cytoplasm the ribosome assembles around it.  The ribosome is composed of two subunits, a small ribosomal subunit and a large ribosomal subunit.  Each of the subunits is composed of rRNA and proteins.  The two ribosomal subunits will bind to the ribosome binding site (rbs) of the mRNA.  The rbs is located prior to the open reading frame of the ribosome. When the ribosome binds to the mRNA the ribosome begins to move down the mRNA.  \n\nDuring this time tRNA is binding to the mRNA as well.  tRNA simply carries the amino acid that will compose the protein to the mRNA so that the amino acids of the protein can become bound to one another.  \n\nSo as the ribosome moves down the mRNA it will encounter tRNA.  However, the tRNA's amino acids will not be bound together until the ribosome reads a mRNA sequeunce that indicates an open reading frame is present. An open reading frame is the sequence of mRNA that is translated into protein sequence.  So once an open readin frame is indicated to be present the ribosome moves down the mRNA until it reaches the start codon.  Protein synthesis begins at hte start codon.  At the start codon the tRNA specifying methionine is present.  Methionine will be the first amino acid in any protein because the methionine codon is also the start codon.  So the methionine tRNA will move into the A site.  At this site the ribosome will ensure that the correct tRNA is bound to mRNA.  If the correct tRNA is bound then the ribosome A site moves onto the next codon and the tRNA just found to be correct will move into the P-site, in this case the methionine tRNA will move into the P-site.  The tRNA that just moved into the A-site will now be checked to see if it is the correct tRNA.  When the tRNA is found to be correct then the amino acid on the tRNA in the p-site will form a peptide bond with the amino acid on the tRNA from the a-site. The amino acid chain is connected to the tRNA in the a-site as the amino acid that was connected to the p-site tRNA becomes disconnected as it forms a peptide bond with the a-site tRNA's amino acid. Then the ribosome moves down the mRNA again.  The tRNA from the p-site moves to the e-site and it is allowed to exit the ribosome.  The p-site and a-site perform the same function as before and the peptide chain will get longer until the ribosome reaches a stop codon.  Once the ribosome reaches a stop codon the peptide chain will no longer increase in size.  The ribosome will then move until it finds another start codon or until the mRNA sequence indicates that it should dissociate.
209909
try\nhttp://web.indstate.edu/thcme/mwking/amino-acids.html