Distinguishing Characteristics:

Ribosomes are typically composed of two subunits: a large subunit and a small subunit. Ribosomal subunits are synthesized by the nucleolus. These two subunits join together when the ribosome attaches to messenger RNA (mRNA) during protein synthesis. Ribosomes along with another RNA molecule, transfer RNA (tRNA), help to translate the protein-coding genes in mRNA into proteins.
Ribosomes: In Journey into the Cell, we looked at the structure of the two major types of cells: prokaryotic and eukaryotic cells. Now we turn our attention to the protein assemblers of a eukaryotic cell, theribosomes. Ribosomes are cell organelles that consist of RNA and proteins. They are responsible for assembling the proteins of the cell. Depending on the protein production level of a particular cell, ribosomes may number in the millions

Location in the Cell: There are two places that ribosomes usually exist in the cell: suspended in the cytosol and bound to the endoplasmic reticulum. These ribosomes are called free ribosomes and bound ribosomes respectively. In both cases, the ribosomes usually form aggregates called polysomes or polyribosomes during protein synthesis. Free ribosomes usually make proteins that will function in the cytosol (fluid component of thecytoplasm), while bound ribosomes usually make proteins that are exported from the cell or included in the cell's membranes. Interestingly enough, free ribosomes and bound ribosomes are interchangeable and the cell can change their numbers according to metabolic needs.

Protein Assembly: Protein synthesis occurs by the processes of transcription and translation. In transcription, the genetic code contained within DNA is transcribed into an RNA version of the code known as messenger RNA (mRNA). In translation, a growing amino acid chain, also called a polypeptide chain, is produced. Ribosomal RNA helps to link amino acids together to produce the polypeptide chain. The polypeptide chain undergoes several modifications before becoming a fully functioning protein. Proteins are very important biological polymers in our cells as they are involved in virtually all cell functions.

aminoacyl-tRNA containing the amino acid methionine, binds to an AUG codon on the mRNA and recruits the large ribosomal subunit. The ribosome contains three RNA binding sites, designated A, P and E. The A site binds an aminoacyl-tRNA; the P site binds a peptidyl-tRNA (a tRNA bound to the peptide being synthesized); and the E site binds a free tRNA before it exits the ribosome. Protein synthesis begins at a start codon AUG near the 5' end of the mRNA. mRNA binds to the P site of the ribosome first. The ribosome is able to identify the start codon by use of the ShineDalgarno sequence of the mRNA in prokaryotes and Kozak box in eukaryotes.

Figure 3 : Translation of mRNA (1) by a ribosome (2)(shown as small and large subunits) into a polypeptide chain (3). The ribosome begins at the start codon of mRNA (AUG) and ends at the stop codon (UAG). In Figure 3, both ribosomal subunits (small and large) assemble at the start codon (towards the 5' end of the mRNA). The ribosome uses tRNA that matches the current codon (triplet) on the mRNA to append an amino acid to the polypeptide chain. This is done for each triplet on the mRNA, while the ribosome moves towards the 3' end of the mRNA. Usually in bacterial cells, several ribosomes are working parallel on a single mRNA, forming what is called a polyribosome or polysome. See also

The ribosome (from ribonucleic acid and the Greek soma, meaning "body") is a large and complex molecular machine, found within all living cells, that serves as the primary site of biological protein synthesis (translation). Ribosomes link amino acids together in the order specified by messenger RNA (mRNA) molecules. Ribosomes consist of two major subunitsthe small ribosomal subunit reads the mRNA, while the large subunit joins amino acids to form a polypeptide chain. Each subunit is composed of one or more ribosomal RNA (rRNA) molecules and a variety of proteins. The sequence of DNA encoding for a protein may be copied many times into messenger RNA (mRNA) chains of a similar sequence. Ribosomes can bind to an mRNA chain and use it as a template for determining the correct sequence of amino acids in a particular protein. Amino acids are selected, collected and carried to the ribosome by transfer RNA (tRNA molecules), which enter one part of the ribosome and bind to the messenger RNA chain. The attached amino acids are then linked together by another part of the ribosome. Once the protein is produced, it can then 'fold' to produce a specific functional three-dimensional structure. A ribosome is made from complexes of RNAs and proteins and is therefore a ribonucleoprotein. Each ribosome is divided into two subunits: the smaller subunit binds to the mRNA pattern, while the larger subunit binds to the tRNA and the amino acids. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. Ribosomes are ribozymes, because the catalyticpeptidyl

Metallic bonding constitutes the electrostatic attractive forces

between the delocalized electrons, called conduction electrons, gathered in an electron cloud and the positively charged metal ions. Understood as the sharing of "free" electrons among a lattice of positively charged ions (cations), metallic bonding is sometimes compared with that of molten salts; however, this simplistic view[which?] holds true for very few[which?] metals. In a more quantum-mechanical view, the conduction electrons divide their density equally over all atoms that function as neutral (non-charged) entities.[citation needed] Metallic bonding accounts for many physical properties of metals, such asstrength, malleability, ductility, thermal and electrical conductivity, opacity, and luster.[1][2][3][4] Although the term "metallic bond" is often used in contrast to the term "covalent bond", it is preferable[by whom?] to use the term metallic bonding, because this type of bonding is collective in nature and a single "metallic bond" does not exist. Metallic bond is not the only type of chemical bonding a metal can exhibit, even as a simple substance. For example, elemental gallium consists of covalently-bound pairs of atoms in both liquid and solid statethese pairs form a crystal lattice with metallic bonding between them. Another example of a metalmetal covalent bond is mercurous ion (Hg2+2)

Strength of the bond:

The atoms in metals have a strong attractive force between them. Much energy is required to overcome it. Therefore, metals often have high boiling points, with tungsten (5828 K) being extremely high. A remarkable exception are the elements of the zinc group: Zn, Cd, and Hg. Their electron configuration ends in ...ns2 and this comes to resemble a noble gas configuration like that of heliummore and more when going down in the periodic table because the energy distance to the empty np orbitals becomes larger. These metals are therefore relatively volatile, and are avoided in ultra-high vacuum systems. Otherwise, metallic bonding can be very strong, even in molten metals, such as Gallium. Even though gallium will melt from the heat of one's hand just above room temperature, its boiling point is not far from that of copper. Molten gallium is therefore a very nonvolatile liquid thanks to its strong metallic bonding. The latter also exemplifies that metallic bonding due to its delocalization in all directions is often not very particular about the directionality of the bonding. There is typically a preference for close packing of the atoms, such as face or body centered cubic arrangements, but in the case of liquid gallium the stacking is not regular, at least not at long range and bond angles are easily changed. Given high enough cooling rates and appropriate alloy composition, metallic bonding can occur even in glasses with an amorphous structure. Much biochemistry is mediated by the weak interaction of metal ions and biomolecules. Such interactions and their associated conformational change has

Solubility and compound formation:

Metals are insoluble in water or organic solvents unless they undergo a reaction with them. Typically this is an oxidation reaction that robs the metal atoms of their itinerant electrons, destroying the metallic bonding. However metals are often readily soluble in each other while retaining the metallic character of their bonding. Gold, for example, dissolves easily in mercury, even at room temperature. Even in solid metals, the solubility can be extensive. If the structures of the two metals are the same, there can even be complete solid solubility, as in the case of electrum, the alloys of silver and gold. At times, however, two metals will form alloys with different structures than either of the two parents. One could call these materials metal compounds, but, because materials with metallic bonding are typically not molecular, Dalton's law of integral proportions is not valid and often a range of stoichiometric ratios can be achieved. It is better to abandon such concepts as 'pure substance' or 'solute' is such cases and speak of phases instead. The study of such phases has traditionally been more the domain of metallurgy than