what does the biuret test of amino acids specify about amino adams in the molecular sense?
91223
Adding a few drops of copper sulphate solution to a protein solution, followed by a few drops of sodium hydroxide solution produces a purple/dark blue precipitate.\n\nIf any protein originally present in the solution has already been changed into amino acids by a protease enzyme for instance, then the precipitate will not appear.\n\nThat should give you a clue about molecules of amino acids compared to molecules of protein. (You might have to remind yourself of the structure of amino acids and proteins.)
554256
methyonin a kind of amino acid
419348
There are twenty standard amino acids:\nhttp://www.chemie.fu-berlin.de/chemistry/bio/amino-acids_en.html\nBut there are also two other non-standard amino acids:\nhttp://en.wikipedia.org/wiki/Amino_acid
213299
SUN's got it right. Iodine is for starch, and biuret is for proteins (or polypeptides that have at least two peptide bonds).\nWhen these indicators react, we can us a spectrophotometer to quantitate how much of whatever substance you're testing for is present.
144967
it has one more carbon in the alkyl chain than arginine
401779
Our body uses amino acids in many ways. When an amino acid is degraded (e.g. phenylalanine to acetyl CoA) ammonia (NH3) is released as a byproduct. Ammonia itself is highly toxic to the human body, however, so we incorporate it into the less toxic urea molecule. Urea has pretty much no other role other than being a nitrogenous waste, and is a component of urine.
919210
The zwitterion structure of glycine means it has two ionic charges on it. So, if you know the fundamental structure of glycine, all you have to do is make sure there is a positive charge on the amino group and a negative charge on the carboxyl group of glycine.\n\nI can't draw out the structure but I'll just write out the formula and maybe that will help.\n\nH3N+--CH2--COO-
294618
Arginine being an aminoacid has a COOH terminus and an NH3 terminus.\nat Ph 7(also called "isoelectric Ph"),all aminoacids become amphoteric.ie,they have both +ve and -ve charge due to ionization of COOH into COO- and NH3 into NH3+.so,when it is protonated,obviously it's COO- group gets neutralized(since proton is added)and gets converted to COOH and now arginine is left with the +vely charged NH3+ grp.THUS it acts as a base.
503574
Amino acid is any molecule that contains both amine and carboxlic acid.  Amino acid is the building block of protein.\n\nVisit http://en.wikipedia.org/wiki/Amino_acid http://en.wikipedia.org/wiki/Amine http://en.wikipedia.org/wiki/Carboxylic_acid
867793
1)That start codon AUG (methionine)\n2) UGG Tryptophan\n\nThose are the only two. All other amino acids have at least two base codes for them and in lots of cases even 4. These codes i have given are mRNA codons.
200416
Aren't you confusing glycine with glutamate?\n\nAnyhow, here is a place that sells glycine.
91071
Acceptor and a donor of ammonia, a compound toxic to the body.\n\nglutamic acid (gltăm´ĭk) is organic compound, one of the 20 amino acids commonly found in animal proteins. Only the L-stereoisomer occurs in mammalian proteins. Like aspartic acid, glutamic acid has an acidic carboxyl group on its side chain which can serve as both an acceptor and a donor of ammonia, a compound toxic to the body. Once glutamic acid has coupled with ammonia, it is called glutamine and can as such safely transport ammonia to the liver, where the ammonia is eventually converted to urea for excretion by the kidneys. Free glutamic acid (that not incorporated into proteins) can also be converted reversibly to α-ketoglutaric acid, an intermediate in the Krebs cycle, and as such can be degraded to carbon dioxide and water, or transformed into sugars. The acidic side chain of glutamic acid confers one negative charge under most conditions to proteins in which this amino acid is found, thus increasing the water solubility of the protein. Monosodium glutamate (MSG), the monosodium salt of L-glutamic acid, is widely used as a condiment. The amino acid was isolated from wheat gluten in 1866 and chemically synthesized in 1890. It is not essential to the human diet, since it can be synthesized in the body from the common intermediate α-ketoglutaric acid.
998721
9\n\n3 bases for each amino acid (applies to both DNA and RNA).
913655
yeah, i agree with what Smokeybon said and some examples of those amino acids are proline, histidine and others look at some shampoo bottles
490305
http://www.biology.arizona.edu/biochemistry/problem_sets/aa/aa.html
1019559
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.
95140
Biuret and proteins have the same response to copper. Copper sulfate is the most common copper salt, so it's used the most.