The sequence of nucleotides determines the sequence of amino acids in proteins. The information for the amino acid sequence of the protein is in the DNA in the nucleus but protein synthesis takes place in the cytoplasm.There are different types of RNA. mRNA is a single-stranded copy of the gene to be translated into a protein and is made in the nucleus but leaves the nucleus through nuclear pores and is used in the cytoplasm.mRNA carries the coded information from the nucleus to the cytoplasm. tRNA helps to assemble the amino acids in the correct order.The complete set of genes of an organism is called its genome. The complete set of proteins is called the proteome.Once the polypeptide chain is synthesised it coils and folds into a secondary structure due to hydrogen bonding between the oxygens of the C=O and the hydrogens of the N-H groups of the peptide bonds. Further coiling and folding due to bonds and interactions between the R-groups occurs and the polypeptide chain forms a tertiary structure.The final protein may have a quaternary structure. More than one polypeptide chain joined together by hydrogen, ionic or covalent bonds may be needed to form the functional protein. Other non-protein molecules may also be needed to form the functional protein.
Protein Synthesis
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Specification: AQA Biology (7401), AS-level, 3.4.2 DNA and protein synthesis. Topic: DNA, Genes and Protein Synthesis.
Key terms in this lesson
- covalent bond
- A strong chemical bond formed when a pair of electrons is shared between two atoms.
- hydrogen bond
- A weak electrostatic attraction between a slightly positive hydrogen atom on one polar molecule and a slightly negative atom, such as oxygen or nitrogen, on another.
- secondary structure
- The coiling or folding of a polypeptide chain, such as into an alpha-helix or beta-pleated sheet, caused by hydrogen bonding between peptide bonds.
- tertiary structure
- The further coiling and folding of a polypeptide into a specific three-dimensional shape, held by ionic bonds, hydrogen bonds and disulfide bridges between R-groups.
- quaternary structure
- The structure formed when two or more polypeptide chains, and sometimes a non-protein prosthetic group, are held together to form a functional protein.
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