tRNA is responsible for bringing individual amino acids to the ribosome in order to be incorporated into the protein. It has an anticodon that attaches to a specific codon found on the mRNA. Once the tRNA and mRNA are bound, a peptide bond if formed between the amino acid residue from the tRNA and the amino acid chain on the ribosome. This is how amino acids are added to the growing protein.

The small subunit of eukaryotic ribosomes is 40S and the large subunit is 60S. These combine to form the ribosome, which is 80S in sedimentary size.

For prokaryotes, the ribosome subunits are 30S and 50S to form a total of 70S total unit.

At the beginning of translation, mature mRNA will travel into the cytosol and attach to the small ribosomal subunit first. This signals the larger subunit to come and attach in order to begin elongation of the polypeptide.

Note that ribosomes do not have an "active site." Active sites are the region of a protein that will bind a substrate and initiate a catalytic change. Ribosomes are not proteins; they are composed of ribosomal RNA (rRNA), and thus do not have active sites.

During translation, the ribosome binds to mRNA and to the appropriate tRNAs. On the ribosome, the mRNA condons are translated into the amino acid sequence of a protein with the help of the tRNA anticodons.

Transcription refers to the synthesis of an RNA molecule from a DNA template. Transformation occurs when a bacterium is able to absorb and incorporate genetic material from the extracellular environment. Transfusion is the transfer of blood from a donor to a recipient. Transfection is the infection of bacteria by phage DNA.

The tRNA carries the amino acid specified by its anticodon. The anticodon base pairs with the codon on the mRNA to ensure the correct amino acid is added to the new protein that is being made. Thus there is a specific tRNA for each codon.

Ribosomes are made up of rRNA and proteins. rRNA synthesis, and ribosome assembly takes place in the nucleolus. 

Transfer RNA—tRNA—is a small folded RNA molecule (i.e. 80-90 nucleotides in length) utilized during translation. On the other hand, tRNA serves as a link between the messenger RNA—mRNA—and the growing protein’s amino acid sequence. The tRNA carries an amino acid to the ribosome directed by the mRNA’s codon—a three-nucleotide sequence. The tRNA carries an anticodon, which is also a three-nucleotide sequence that matches the genetic code, which complements the mRNA. Last, rRNA is associated with the ribosome. 

Ribosomes are responsible for translating mRNA into protein. tRNA molecules transport amino acids to the ribosome, where they are joined by peptide bonds to form a chain. This chain of amino acids is known as the protein primary structure.

Secondary structure, tertiary structure, and quaternary structure form in the cytoplasm or endoplasmic reticulum after the ribosome has released the polypeptide.

Proteins have four levels of structure. Secondary structure involves the formation of alpha-helices and beta-sheets via hydrogen bonding between the amino acid backbone in the protein chain.

Primary protein structure simply refers to the linear sequence of amino acid residues in the polypeptide chain. After initial folding of the backbone in secondary structure, functional groups of the amino acids interact to generate tertiary structure. Tertiary structure contains hydrogen bonding, hydrophobic interactions, and disulfide bridges. Some proteins then develop quaternary structure, when multiple polypeptide chains are joined as subunits to build a large protein complex.

Formation of a protein involves four distinct levels of structure. The tertiary structure is the third level of protein formation, and occurs when the side chains of the individual amino acids interact. These side chains can attract one another to form hydrogen bonds or disulfide bonds, or they can repel each other and contribute ot hydrophobic interactions. The result is a three-dimensional shape. This is the final level of structure to create a function protein subunit.

The primary structure of the protein is derived from the chain of amino acids synthesized during translation; this amino acid sequence is the primary structure. Secondary structure is generated from the interactions between amino and carboxyl groups in the polypeptide backbone. These groups can form hydrogen bonds to generate alpha-helices and beat-pleated sheets. Tertiary structure, as described above, results in a functional protein subunit. For some protiens, tertiary structure is the final step in folding. For other proetins, multiple subunits can be bound together to generate a quaternary structure.