What the role of tRNA in protein synthesis?
157202
tRNA are called transferRNA. Their job is to match the codons at the site of DNA translation (ribosomes) with their anti-codon on one side and on the other side of tRNA is the Amino Acid that the codon codes for.
17613
Through a process called translation in which the information contained in nucleic acids (DNA & RNA) are converted into a protein sequence. This process is done on piece of cellular machinery called the ribosome.
217097
Messenger RNA (mRNA) is RNA that encodes and carries information from DNA during transcription to sites of protein synthesis to undergo translation in order to yield a gene product.\n\nTransfer RNA (abbreviated tRNA) is a small RNA chain (74-93 nucleotides) that transfers a specific amino acid to a growing polypeptide chain at the ribosomal site of protein synthesis during translation. It has sites for amino-acid attachment and codon (a particular sequence of 3 bases) recognition. The codon recognition is different for each tRNA and is determined by the anticodon region, which contains the complementary bases to the ones encountered on the mRNA.\n\nRibosomal RNA (rRNA) is the primary constituent of ribosomes. Ribosomes are the protein-manufacturing organelles of cells and exist in the cytoplasm. rRNA is transcribed from DNA, like all RNA. Ribosomal proteins are transported into the nucleus and assembled together with rRNA before being transported through the nuclear membrane. This type of RNA makes up the vast majority of RNA found in a typical cell. While proteins are also present in the ribosomes, solely rRNA is able to form peptides. Therefore ribosome often is referred to as ribozyme.
6965
Initiation of translation depends on the sequence around the start codon as well. The translation machinery looks for a consensus sequence that stabilizes binding. I believe false starts can lead to aberrant transcripts, which would be degraded. The start methionine may be the first in the mRNA transcript, but doesn't have to be. As previously mentioned, an AUG in the open reading frame codes for methionine.
254108
When a protein is synthesized at a ribosome, it travels to the endoplasmic reticulum to get modified and packaged. Then it travels to the Golgi Apparatus, which gets the protein ready for leaving the cell.\n\nSo both the ER and the Golgi Apparatus package the protein to help it leave the cell.
289641
Yes.  DNA is transcribed into RNA, and RNA is translated into proteins.  \n\nI always kept that straight by thinking of transcription as like taking notes when someone is talking (same language) and translation as translating those notes into another language.  Going from DNA to RNA you're going to use the same building blocks (bases - purines and pyrimidines)or the same "language", but going from RNA to proteins requires going from one building block to another (bases to amino acids), or a different language.
781789
mRNA is the RNA that carries information during transcription and translation. It has codons, which match up with the anticodons on tRNA. tRNA is the RNA that bonds to amino acids and transfers them to ribosomes, and mRNA. The reason RNA is used is because the cytoplasm is too damaging to DNA, so RNA is kind of a scapegoat. Hopefully, this helps.
81856
All answers are correct. The primary aminoacid sequence is changed which may have implications for the structure and funtion of the protein
304478
Proteins are composed of one or more polypeptides and polypeptides are a sequence of amino acids. every polypeptide is coded by a particular gene. during polypeptide synthesis, dna unwinds and one strand acts as a template (which is possible because of the complementary base pairs). spare bases are used to form  messenger RNA (mRNA) using the template. the mRNA moves out of the nucleus and into the cytoplasm towards the ribosomes. at the ribosomes, the polypeptide is actually synthesised. tRNA consists of an anticodon (sequence of three bases) and an amino acid. It matches its anticodon to the appropriate codon (sequence of three bases) to the mRNA. this continues with different tRNA molecules until a sequence of amino acids are formed- thus creating a polypeptide. \n\nSo, since proteins consists of polypeptides which are formed by the information in genes, in essence, a protein's structure and function is determined heavily by the gene that synthesises it.
251912
The statement is true. If you assume that takeing dna to rna is the same language, then that would be transcribing, while rna to prtien is a different language, that is translating
712715
The uracil in the RNA helps in "wobbling" - Wobbles base pairing when mRNA and tRNA bind - protein synthesis
214091
Transcription is when the nucleus of a cell wants to send a "message" for a protein (polypeptide chain) to be made. It copies this "message" from part of the DNA onto an m(essenger)RNA strand, in which the Thymine of the DNA is now the Uracil of the RNA.\n\nex) DNA message: TAC CGG TAA\n           mRNA: AUG GCC AUU\n\nAfter that is translation, where the message from mRNA gets read by the ribosome to build a polypeptide chain that will eventually become a protein!
503387
first of all proteins  are  synthesized by the  combination of many things on the  ribosomes in the  cytoplasm not  in the  DNA\nit is  a very complicated process but here is  a simplification of it:\nA)translation---->\n1-DNA double strand opens up by a  certain specific molicule (like  unzipping the DNA) this is  controled by an initiator and inhibitor and so many other molecules due to the dec or inc of certain specific molecule in the cells\n2-RNA single strand is formed over one of the double strand DNA (G-C A-T or U) ending up in what we call messenger-RNA this mRNA separates from the original DNA strand by a very complicated process involving so many  chemical  molecules  and  leaves the nuclease through pores in the nuclear membrane\nB)transcription--->\n1-the mRNA reaches to ribosomes either on the Endoplasmic reticular systems outer surface or free in the cytoplasm(ribosomes are composed of two protein subunits one big  and one small) the mRNA incers inside between  the two parts of ribosomes \n2- ribosomes start reading the mRNA as Codones (triple sequences) like ACG-AUC-CUA-AAA\n3- for each codon sequence there is  a specific molecule in the cytoplasm that called transcription-RNA which attaches one codon from one specific codon from one side and one specific amino acid from the other side \n4-so at this stage we find  a sandich of aminoacids on top tRNA in the middle and mRNA on the other side\n5- finally these amino acids will all connected togather and separat from the ribosome and the sandwich \nNOTE: so actually every single codon has a single part of tRNA that will specificly attach to it and attach  a specific amino acid from the other  end and thats what they meant by discovering the human genome (knowing each  codon goes with what  part of tRNA and each part of tRNA goes with what amino acid\nC)modification---->\n1-now the protein is a  simple sequence of amino acids with no 3 dimentional structure \n2-modification is  a whole  very  complicated process that cant be writen in here but it involves golgi aparatus smooth endoplasmic reticulum and rough endoplasmic reticulum\nFINITO
826034
One tRNA is needed for each tri-nucleotide in the RNA that is being transcribed, so in theory 64 would be needed to ensure any RNA could be translated. However there is some bias in codon usage (some tri-nucleotides are not found in certain species) so in practice you would need slightly less than this. Of course if the protein being translated did not contain all 20 amino acids less would also be required then
93102
the functions are:\nmRNA: Carries information and goest to ribosomes\ntRNA: Goes to the cytoplassm and picks up the amino acids\nrRNA: Makes the ribosomes
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.
670967
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.