The larger subunit is where the transfer tRNA is located. The tRNA is a form of RNA, which is thought of as the connection between the amino acid sequence of proteins and the nucleoside sequence. It does this by carrying the relevant amino acid, to the complementary codon on the mRNA, as directed by the codon itself.
Structurally, the tRNA is an L shaped structure, whereby the anti codon is on one end, and the amino acid is adjacent to the anti codon. The smaller subunit of the ribosome, is comprised of the mRNA. The Trna is responsible for locating and finding the amino acids and taking them to the ribosome, prior to translation.
Translation is the process by which the m RNA is interpreted, whereby the instructions are read, by which proteins are assembled. There are initially three steps in the translation process.
The initiation step starts by the m RNA biding to the ribosome structure. It binds to the specific location by means of initiation factors; these are a group of other proteins, which help the Mrna bind to the correct location on the ribosome smaller subunit. It is here that the mRNA will present the genetic code order for constructing a protein, by means of a codon.
A codon is a series of three nitrogenous bases, with each amino acid of a protein represented by this codon. Codons are the key to the lock; the lock being the anti codon, by which is the complementary set of nitrogen...
... middle of paper ...
...e. Whereby the polypeptide will bend, foil or coil. The tertiary structure is where two or more polypeptides join together, via a variety of different bonds such as, hydrogen, disulphide bonds, ionic and covalent bonds. The quaternary structure of proteins will be the three dimensional structure of the protein, in its final stage. Here it will have completed its folding, and will be a globular shape. An example being,
There are enzymes called chaperones, which aid the protein to fold at each end of the protein together, chaperones, simply help to absolute this task. However, protein folding can also be adjusted by means of other modifications, such as disulphide bonds. These bonds will fasten two parts of the polypeptide jointly together. Another alteration is via phosphate groups, these are the most abundantly used, to alter the structure of the protein.
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