The Building Blocks: What are Amino Acids?
At the most fundamental level, proteins are made by joining repeating units of smaller organic molecules called amino acids. An amino acid consists of a central alpha ($\alpha$) carbon atom bonded to four different groups: a hydrogen atom, an amino group ($-NH_2$), a carboxyl group ($-COOH$), and a variable side chain (denoted as the R-group). There are 20 standard amino acids that are used to build the vast array of proteins found in living organisms. The chemical properties of the protein, including how it folds and functions, are determined by the specific sequence and characteristics of these R-groups.
The Peptide Bond: Linking Amino Acids Together
To form a protein, amino acids are joined together in a linear chain through a covalent linkage known as a peptide bond. This occurs via a dehydration synthesis (or condensation) reaction, where the carboxyl group of one amino acid reacts with the amino group of the next, releasing a molecule of water. The resulting chain of amino acids is called a polypeptide. During protein synthesis within a cell's ribosomes, this process repeats, adding amino acid after amino acid to the growing polypeptide chain according to the instructions encoded in messenger RNA (mRNA).
From Polypeptide Chain to Functional Protein
Once the polypeptide chain is complete, it is not yet a functional protein. It must fold into a specific three-dimensional structure to carry out its biological role. This complex folding process gives rise to four levels of protein structure:
- Primary Structure: The linear sequence of amino acids in the polypeptide chain. It is determined by the genetic code and is the basis for all higher-level structures.
- Secondary Structure: Local, folded patterns within the polypeptide chain, such as $\alpha$-helices and $\beta$-pleated sheets. These are formed and stabilized by hydrogen bonds between the atoms of the polypeptide backbone.
- Tertiary Structure: The overall, unique three-dimensional shape of a single polypeptide chain. This compact structure is formed through interactions between the amino acid side chains, including hydrogen bonds, ionic bonds, disulfide bridges, and hydrophobic interactions.
- Quaternary Structure: The arrangement of multiple polypeptide chains (subunits) into a single functional protein complex. Not all proteins have a quaternary structure; examples include hemoglobin, which is composed of four subunits.
The Cellular Machinery of Protein Synthesis
The process of creating proteins is carefully orchestrated within the cell and involves several key players:
- DNA: Contains the master blueprint for all proteins. The sequence of nucleotides in a gene dictates the amino acid sequence of a particular protein.
- Transcription: An enzyme called RNA polymerase reads the gene on the DNA and creates a messenger RNA (mRNA) molecule.
- mRNA: Carries the genetic message from the DNA in the nucleus to the ribosomes in the cytoplasm.
- Ribosomes: Act as the cellular factory where the protein is actually built. They read the mRNA sequence and catalyze the formation of peptide bonds between incoming amino acids brought by tRNA.
- tRNA: Transfer RNA molecules act as adaptors, bringing the correct amino acid to the ribosome based on the mRNA code.
Comparison of Protein Types by Molecular Shape
Proteins can be broadly classified based on their final, folded molecular shape, which directly impacts their function.
| Feature | Globular Proteins | Fibrous Proteins |
|---|---|---|
| Shape | Compact, spherical or rounded. | Long, narrow, and rod-like. |
| Solubility | Generally soluble in water. | Typically insoluble in water. |
| Function | Metabolic processes (e.g., enzymes, hormones, antibodies). | Structural and mechanical support (e.g., collagen, keratin). |
| Structure | Complex folding, often with a hydrophobic core and hydrophilic exterior. | Parallel polypeptide chains held together by cross-links. |
| Example | Insulin, Hemoglobin. | Collagen, Keratin. |
The Significance of Correct Protein Folding
The final shape of a protein is critical for its function. A single mistake in the amino acid sequence can cause a protein to fold incorrectly, leading to a loss of function and potentially serious diseases. For example, the genetic defect causing sickle cell anemia is a single point mutation that changes one amino acid in the hemoglobin protein, leading to its aggregation and the characteristic sickling of red blood cells. In other cases, misfolded proteins can form harmful aggregates linked to neurodegenerative disorders like Alzheimer's and Parkinson's disease. The cell has a system of chaperone proteins to assist with proper folding, but errors can still occur.
Conclusion
In summary, the answer to what are proteins made by joining is amino acids. This process, driven by the genetic code and facilitated by ribosomes, creates long polypeptide chains linked by peptide bonds. These chains then undergo intricate folding into precise three-dimensional structures, which are essential for their biological function. From providing structure and catalyzing reactions to transporting molecules and defending the body, the vital work of proteins is a testament to the elegant efficiency of combining simple building blocks to create molecular complexity. Understanding this fundamental process is key to comprehending not only how life works but also how diseases can arise from errors in this intricate biological assembly line. For more detailed information on proteins and their structure, consult the NCBI Bookshelf page on "The Shape and Structure of Proteins".