Protein | Structure | Function & Responsibilities | Key Amino Acids (Examples) | Bond Types | Active Sites | Associated Medicines |
Approx. No. of Amino Acids
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Hemoglobin | Quaternary (four subunits) | Transports oxygen from lungs to tissues and removes carbon dioxide from tissues. | Heme (contains iron), Histidine | Peptide bonds (within each subunit), Hydrogen bonds (between subunits) | Heme group in each subunit | None directly associated with hemoglobin structure |
~574 (per subunit)
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Insulin | Globular | Regulates blood sugar levels by facilitating glucose uptake by cells. | Cysteine (forms disulfide bonds) | Peptide bonds, Disulfide bonds | Receptor binding site | Insulin itself is a medication for diabetes | ~51 | Explore in Uniprot | ||
Collagen | Fibrous | Provides structural support to skin, bones, tendons, and ligaments. | Glycine, Proline, Hydroxyproline | Peptide bonds, Hydrogen bonds, Cross-links (e.g., covalent bonds between lysine residues) | Not applicable (primarily a structural protein) | Vitamin C deficiency affects collagen synthesis (Scurvy) |
~1000 (varies by collagen type)
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Antibodies | Y-shaped | Bind to foreign substances (antigens) and neutralize them, playing a crucial role in the immune response. | Variable regions with diverse amino acid sequences for antigen binding | Peptide bonds, Disulfide bonds | Antigen-binding sites (variable regions) | Immunoglobulins (antibodies) themselves are used as therapeutic agents | ~1300-1500 | Explore in Uniprot | ||
Actin | Filamentous | Major component of the cytoskeleton, involved in cell movement, muscle contraction, and cell division. | Actin-specific amino acids involved in polymerization | Peptide bonds, Non-covalent interactions (e.g., hydrophobic interactions) | Myosin binding sites | Medications that target muscle contraction (e.g., muscle relaxants) may indirectly affect actin-myosin interactions | ~375 | Explore in Uniprot | ||
Myosin | Filamentous | Interacts with actin to generate force for muscle contraction. | Myosin head contains ATP-binding site and actin-binding site | Peptide bonds, Non-covalent interactions | Actin-binding site, ATP-binding site | Medications that target muscle contraction (e.g., muscle relaxants) may indirectly affect actin-myosin interactions |
Varies greatly depending on the myosin type (e.g., ~1900 for myosin II)
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Enzymes (e.g., lysozyme) | Globular | Catalyze biochemical reactions by speeding them up without being consumed in the process. (e.g., lysozyme breaks down bacterial cell walls) | Active site contains specific amino acids for substrate binding and catalysis | Peptide bonds, Hydrogen bonds, Hydrophobic interactions | Active site (contains catalytic residues) | Many medications target enzymes (e.g., enzyme inhibitors used to treat various diseases) | ~129 | Explore in Uniprot | ||
Membrane proteins | Integral or peripheral | Transport molecules across cell membranes, act as receptors for signals, and participate in cell-to-cell communication. | Hydrophobic amino acids for membrane insertion, specific amino acids for ligand binding | Peptide bonds, Hydrophobic interactions (for integral proteins) | Ligand-binding sites (for receptor proteins), Channel pores (for transport proteins) | Many medications target membrane proteins (e.g., beta-blockers, which target receptors in the heart) |
Highly variable (can range from a few dozen to thousands)
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Keratin | Fibrous | Provides strength and resilience to hair, nails, and skin. | High in cysteine (forms disulfide bridges) | Peptide bonds, Disulfide bonds | Not applicable (primarily a structural protein) | None directly associated with keratin structure |
Varies greatly depending on the keratin type (e.g., ~310 for alpha-keratin)
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Elastin | Fibrous | Provides elasticity and flexibility to tissues such as blood vessels and lungs. | Rich in glycine and proline | Peptide bonds, Cross-links (desmosine) | Not applicable (primarily a structural protein) | None directly associated with elastin structure | ~800-1000 | Explore in Uniprot | ||
Casein | Globular | Major protein in milk, provides nutrition for infants. | Phosphorylated amino acids | Peptide bonds, Hydrogen bonds, Phosphoryl groups | Not applicable (primarily a nutritional protein) | None directly associated with casein structure | ~200 | Explore in Uniprot | ||
Albumin | Globular | Major protein in egg white, provides nutrition and protection to the developing embryo. | Contains a variety of amino acids | Peptide bonds, Hydrogen bonds, Hydrophobic interactions | Not applicable (primarily a nutritional protein) | None directly associated with albumin structure | ~585 | Explore in Uniprot | ||
Rhodopsin | Globular | Pigment in the retina, essential for vision by absorbing light. | Contains retinal (a light-absorbing molecule) | Peptide bonds, Hydrogen bonds, Hydrophobic interactions | Retinal binding site | Medications for eye diseases (e.g., glaucoma) may indirectly affect retinal function | ~348 | Explore in Uniprot | ||
Histones | Globular | Package and order DNA into structural units called nucleosomes, helping to regulate gene expression. | Rich in lysine and arginine (positively charged) | Peptide bonds, Hydrogen bonds, Ionic interactions (between positively charged histones and negatively charged DNA) | DNA binding sites | Medications that affect gene expression may indirectly influence histone interactions with DNA |
~102-130 (varies by histone type)
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GFP (Green Fluorescent Protein) | Beta-barrel | Used as a fluorescent tag in biological research to visualize specific proteins or cellular structures. | Contains chromophore responsible for fluorescence | Peptide bonds, Hydrogen bonds, Hydrophobic interactions | Chromophore | None directly associated with GFP structure | ~238 | Explore in Uniprot |
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