which element do amino acids have that carbohdrates & lipids do not? what do the group NH2 found in amino acid
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emm...is this your homework??well..it seems that the question is not from you (individually). Hmm..for more understanding, check out this website:\n\nhttp://faculty.clintoncc.suny.edu/faculty/Michael.Gregory/files/Bio%20101/Bio%20101%20Lectures/Biochemistry/biochemi.htm\n\nI hope it solves your dillema, good luck :)
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What the above guys are talking about is valence, as far as I know there are no nitrogen ions, an ion is a charged particle, that has completely taken or given up electrons but DOES NOT share them, for example the chloride ion. However all of the nitrogen compounds I know (and I must accept I don't know it all) share their electrons
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Liquid Nitrogen: N2\n\nThe diatomic elements are hydrogen, nitrogen, oxygen, and the halogens: fluorine, chlorine, bromine, iodine, and astatine. Astatine is so rare in nature (its most stable isotope has a half-life of only 8.1 hours) that it is usually not considered. Many metals are also diatomic when in their gaseous states.\n\n\n\nIn inorganic chemistry, the bisulfite (IUPAC-recommended nomenclature: hydrogen sulfite) ion is the HSO3− ion. It is the conjugate base of sulfurous acid, H2SO3. Salts containing the \nHSO3− ion are bisulfite [salt]s It is a weakly acidic substance which has a pKa of 6.97.\n\nSilver Bisulfate: AgHSO3\n\n\nPotassium Phospate (tribasic): K3 P O4 \n\nhttp://www.hbci.com/~wenonah/hydro/2kpo.htm
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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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Amino acids are organic molecules with amino groups (-NH2) and acidic groups (-COOH).  When the amino group (-NH2) of one amino acid reacts with the acidic group (-COOH) of another, the bond is called a "peptide" bond (IIRC.)\n\nIf you link a small number of amino acids in this way, the product is often just called a "peptide".  The better term is "oligopeptide", as "oligo" comes from Greek, meaning "few".\n\nReally long peptides are called polypeptides or proteins.  ("poly" comes from Greek, too, meaning "many")\n\nSome proteins have different polypeptides that stick together, held by weaker forces such as electrostatic attraction.\n\nDoes that help?
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Triglycerides.\n\nNucleotides, Amino acids and Carbohydrates are soluble in water, and can thus not be hydrophobic by definition.
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The amino and carboxyl protons are very difficult to observe. Using 100% D2O will replace the carboxyl and amino protons with 2H, and you won't see anything. Use a different solvent and you can't be sure you are in the zwitterion form (pH is difficult to control in non-aqueous solutions and you will get different hydrogen bonding)\n\nIf you really want to see those protons your best bet would be to use 90% H2O / 10% D2O with either phosphate buffer or the perdeuterated buffer of your choice (you can get these from Cambridge Isotopes). Make sure the buffer concentration is large compared to your amino acid, and make sure you have adjusted the pH to the zwitterion range. When you aquire the spectrum you will need to use a water suppression sequence. Presat is the easiest, although I much prefer gradient selected 3-9-19. This still may not be enough to see the protons-- if they are exchanging the linewidth may become so broad as to disappear into the baseline.\n\nWhile it's difficult to observe the carboxyl and amino protons (they are *very* sensitive to solvent and pH) you should be able to see changes in the chemical shifts of the remaining protons, particularly the alpha protons.\n\nIf you are really interested, make a sample of your favorite amino acid and take spectra over a range of pH. Plot the chemical shifts of the visible protons as a function of pH and the shape of the curve should allow you to determine the pKa of the amino and carboxyl groups. Here you could get away with just using D2O, which makes the spectroscopy much simpler.\n\nGood luck and have some fun with this!
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Vegetables contain all of these organic compounds in differing amounts.  Carbohydrates as both sugars and copious amounts of cellulose.  Proteins in the cells, but not generally as large structual components (obviously no huge protein sinks like muscles.)  Lipids as cell membranes etc....  All living things have nucleic acids, even viruses.
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The two major classes of molecules in our body: \n1. Organic: these are any molecules that have carbon atoms in them, like proteins, carbohydrates, and nucleic acids (DNA, RNA).  \n2. Inorganic: these are any molecules that do not have carbon atoms in them, like water and minerals.
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In proteins and peptides the nitrogen group is reacted with the carboxylic group beside it, with only the very last (or very first) amino acid in the protein/peptide chain being free, where as in amino acids all of the amine groups are free.
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Proteins, amino acids.
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All other common amino acids have a primary amino group. The primary amino group is essential for the formation of the purple chromophore.\nProline has a secondary amino group so the reaction is different\n\nHave a look at the link below
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The amino acids that go into making proteins are so-called alpha-amino acids. This is because they have an amino group (-NH2) on the carbon atom just next to the carboxyl group (-COOH). The simplest such amino acid is glycine, H2N-CH2-COOH. Another simple one is alanine, CH3-CH(-NH2)-COOH (three carbons, the NH2 group on the second one). There are about 22 amino acids that go into the making of proteins. Some are essential: This means that the body cannot make them, and they are needed in the diet. Others are nonessential: The body can make glycine and alanine from other raw materials.
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http://www.lloydminsterheavyoil.com/nitrogen.jpg\nhttp://www.tcm.phy.cam.ac.uk/castep/MD/img43.png
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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.
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This would be (d).\n\nThe presence of an amide bond (R-NH-CO-R) is the main part of a peptide bond.\n\nB may look like this too, however in a peptide bond, but the amino group should be on the alpha-carbon of an amino acid.
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amino acids; this giant molecule mainly constructed from carbon, oxygen, nitrogen and hydrogen atoms.