What are the three key elements that are required in assembling the protein chain?
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You need mRNA to act as a template, ribosomes to catalyze the reaction and tRNAs carrying the amino acids which will make the protein chain. Actually you need more stuff like GTP but these 3 are the basics.
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Well, There are 20 different amino acids that are required for normal function to form proteins. They are divided into four different groups: non-polar amino acids, polar amino acids, aromatic amino acids and positively charged amino acids, depending on their side chains
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a primary protein is one that has peptide bonds linking the amino acids.\nin  a secondary protein, the protein chain folds upon itself with hydrogen bonds.\nin a tertiary protein, folding also occurs but with stronger sulphide and nitrogen bonds\nin a quartenary protein, two protein chains bond together to form a protein
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1. periodic table (?), 2. nucleotides, bases,  3. fatty acids,  6. saturated fatty acid, trans fat,  8. energy (?), 12. adenosine diphosphate (ADP)
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amino acids; this giant molecule mainly constructed from carbon, oxygen, nitrogen and hydrogen atoms.
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During protein synthesis, 20 different amino acids can be incorporated in proteins. After translation, the posttranslational modification (PTM) of amino acids extends the range of functions of the protein by attaching to it other biochemical functional groups such as acetate, phosphate, various lipids and carbohydrates, by changing the chemical nature of an amino acid (e.g. citrullination) or by making structural changes, like the formation of disulfide bridges.\n\nPTMs involving addition include:\n\nacetylation, the addition of an acetyl group, usually at the N-terminus of the protein \nalkylation, the addition of an alkyl group (e.g. methyl, ethyl) \nmethylation the addition of a methyl group, usually at lysine or arginine residues. (This is a type of alkylation.) \nbiotinylation, acylation of conserved lysine residues with a biotin appendage \nglutamylation, covalent linkage of glutamic acid residues to tubulin and some other proteins. \nglycylation, covalent linkage of one to more than 40 glycine residues to the tubulin C-terminal tail \nglycosylation, the addition of a glycosyl group to either asparagine, hydroxylysine, serine, or threonine, resulting in a glycoprotein \nisoprenylation, the addition of an isoprenoid group (e.g. farnesol and geranylgeraniol) \nlipoylation, attachment of a lipoate functionality \nphosphopantetheinylation, the addition of a 4'-phosphopantetheinyl moiety from coenzyme A, as in fatty acid, polyketide, non-ribosomal peptide and leucine biosynthesis \nphosphorylation, the addition of a phosphate group, usually to serine, tyrosine, threonine or histidine \nsulfation, the addition of a sulfate group to a tyrosine.
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There are four structures; primary, secondary and Tertiary structures. \n\nThe primary structure is the sequence of amino acids in a polypeptide chain, held together by peptide bonds (which occur between the amine group of one amino acid and the carboxyl group of another). \n\nThe secondary structure is the folding of the polypeptide chain into alpha helices and Beta pleated sheets, these are held together due to hydrogen bonding within the polypeptide itself. \n\nTeritary structure is the further folding of a polypeptide chain into a complex globular molecule (also held together by hydrogen bonds).\n\nFinally, Qauternary structure is the folding of two polypeptide chains together, the two chains are held together not only by hydrogen bonds but also by ionic bonds and disulphide bridges(these bonds form between the suplhur atoms on the R groups of the amino acids).
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Amino acids.  All proteins are combinations of only these twenty amino acids, which are known as the building blocks of proteins.  The listed source can give you a list of the twenty amino acids.
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Presumably you know that the primary structure of a protein is simply a chain of amino acids.  The secondary and tertiary structures form as the result of various intermolecular forces pulling different amino acids in that chain together.  Hydrogen bonding is one of the intermolecular forces that act on the amino acids in the chain and cause them to fold up. Think of it this way: if you started with a long strip of paper (representing the primary structure of the protein), and then stapled it together in a bunch of places to make a complicated three-dimentional structure, the hydrogen bonds would be like the staples (or some of them), holding the linear chain of amino acids in a three-dimentional shape.
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The proteins shape determines its function.  Most proteins have to bind to something else in order to do its job.  If it's not a specif shape, it can't bind.
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Carbohydrates, Fats, Vitamins, Proteins, Minerals, Water
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Yup, Ribosomes. Ribosome is an organelle in cells that assembles proteins. Ribosomes are composed of ribosomal RNA and ribosomal proteins . It translates messenger RNA (mRNA) into a polypeptide chain It can be thought of as a factory that builds a protein from a set of genetic instructions. Ribosomes can float freely in the cytoplasm  or bind to the endoplasmic reticulum, or to the nuclear envelope.
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The answer is A, translation.\n\n\nDuring translation, the messenger RNA copies information from DNA to produce proteins. The information gets read by  ribosomes which facilitate the production of proteins.
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DNA\nRNA\ncarbohydrate (eg glycogen)\npolypeptides (proteins)\nmucopolysaccharides (proteins joined to carbohydrates)\nlipopolysaccharides (proteins joined to lipids)\nother lipids eg in membranes, and storage fat\n\nThere may be others.
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Well this is a good question.\nIt depends on how much expenses you can afford and what are the technical expertise available with you\nAny ways here I offer you a few tips which you could think on.\n\nI will suggest you to use thermocol or a trasperant material for building up your ribosome model.\n\nAs its structure is very simple, cut two pices of thermocol as small and large subunits and paint them with two different \n\ncolours. Here you can use a combinations of model. Use this first one as a intact one to demonstrate just the shape of it. \n\nNow you can cut the thermocol in two different peices and show them as two subunits and explain it very briefly.\n\nHaving done so you can now expalin the intrinsic appearance and structure.You can show A, P and E sites which are L shaped and its easy to make. Becasue you can cut and carve the thermocol as you wish.\n\nIn the next model you can show the translation process. Use a wire as mRNA and show how it binds to above three \n\nmentyiones sites and show the amino acids coming out as small plastic beads coated to the wire.\n\nTo make your model more impressive, use a sheet of paper and display on your stall or board. This will help you for a better \n\ncommunication. Use this sheet for explaination of model. You can draw figures on this sheet and correlate the information with \n\nyour hand made model. This should go well.\n\n\nAlso add information of mRNA and riboseme, difference of prokaryotic and eucaryitic ribosome as a samll table. Arrange all the \n\ninformation carefully on the sheet and explain it as well.\nYou may find it exhaustive but I assure you this will get you good applauses.\n\nBye \n\nRavi
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Here's a good site:http://www.accessexcellence.org/RC/VL/GG/protein_synthesis.html\n\nAnd here another with a movie to explain it:http://www.lewport.wnyric.org/jwanamaker/animations/Protein%20Synthesis%20-%20long.html
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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.