Protein Structural Consideration
With the variety of amino acids that can be incorporated in the structure of a protein molecule, protein can exhibit different structural properties. The difference in the structural properties enables proteins to serve different structural functions. Common structural proteins in an organism include the following: keratins in hair and nails; collagen in cartilage and connective tissues; fibroin in silk; elastin and fibrillin in connective tissues; lamin in the nuclear envelope; actin in cytoskeleton filaments; and tubulin in microtubules. These proteins serve different structural functions and have different structural properties owing from the difference in their amino acid components.
The primary structure of a protein involves the formation of peptide bonds between amino acids. The amino acid sequences for a specific protein are encoded in DNA. The side chains of amino acids enable different types of interaction within the molecule. These interactions cause the protein molecule to produce different secondary and tertiary structures. The chemical and biological properties of proteins depend more on their three-dimensional or tertiary structure.
The secondary structure of proteins may form hydrogen bonding within the molecule. This hydrogen bonding pushes the protein molecule to form structural conformations, namely α-helix and β-sheets. The α-helix is a right-handed coiled strand, while the β-sheet involves protein strands lying side by side connected on different parts of its structure by hydrogen bonds.
The tertiary structure of protein determines its over-all three-dimensional shape. A protein molecule tends to bend and twist so as to achieve maximum stability. The stabilizing forces are the bonding interactions between amino acid side chains. Due to the solvent polarity around the protein molecules, hydrophobic amino acids tend to be buried in the interior of the protein molecule. Acidic and basic amino acids are the ones generally exposed because of their high hydrophilicity.
Proteins that serve different structural functions are divided into two types: fibrous and globular. Fibrous proteins are proteins that have thread-like structure. They may have normal helical or sheet structure; they exhibit comparatively stronger intermolecular forces of attraction. They are also relatively insoluble in water, acids and bases. Globular proteins, on the other hand, have folded ball-like structure. Weak intermolecular hydrogen bonding governs in the structure of this type of proteins. They are also soluble in water, acids and bases.
Fibrous proteins mostly exhibit just secondary structures. Repeat sequences are also common in the structure of fibrous proteins. Most of the chains of amino acids may be linked by disulfide bridges. This disulfide linkage makes the protein very strong and stable. The most common fibrous proteins are collagen and keratin. Collagen is found in bone, cartilage, tendons and ligaments. This fibrous protein is strong, but is still very flexible. The repeat sequence for collagen is glycine-proline-X (any other amino acid). The combination of amino acids enables the collagen to be wound in tightly-coiled, straight or unbranched helices.
Globular protein changes conformation in such a way that the hydrophobic groups are inside the core of the protein, while the hydrophilic groups are exposed. This arrangement makes globular protein very soluble. The most common globular protein is hemoglobin. Hemoglobin is used to transport oxygen around the body. Its quaternary structure is made up of 4 polypeptide chains; two of which are identical alpha chains with 141 amino acids. The other two are identical beta chains with 146 amino acids. The four chains are linked to form a roughly spherical molecule. Attached to each of the polypeptide chain is a Fe2+ ion which can combine with one O2 molecule. Since there are 4 polypeptide chains, a maximum of four O2 molecules can be transported by a hemoglobin molecule.
Communication and Signaling
Cell signaling is a part of a complex communication system that regulates cell activity and coordinates cell actions. How cells respond to the microenvironment is the basis for its development, for tissue repair, and for immune response. Two of the primary functions of proteins in communication and signaling are as membrane receptors and as peptide hormones.
Membrane proteins are proteins that interact with, or are part of, the biological membranes. They may be permanently anchored on it or only temporary attached to the lipid bilayers. Membrane proteins may serve a variety of functions. In terms of communication and signaling, proteins can serve as membrane receptors which can relay signals between the cell’s internal and external environments. They may serve as transporters, channels, linkers and as receptors. As receptors, proteins enable the binding of specific ligands. Cell-surface receptors are divided into three general categories: ion channel-linked receptor; G-protein-linked receptor and enzyme-linked receptor. Ion-channel linked receptor bind a ligand enabling conformational changes that open the channel to allow specific ions to pass through. G-protein-linked receptors bind a ligand and activate a membrane protein called a G-protein. This then interacts with either an ion channel or an enzyme in the membrane. Enzyme-linked receptors are receptors associated with an enzyme.
Proteins involved in Movement
Another important function of proteins is its involvement in cell movements. Microtubules are part of the mechanism for cell movement. Movement along the microtubule length is dependent on the action of motor proteins in it. These proteins utilize energy from ATP hydrolysis to produce movement. Two families of motor proteins are responsible for the cellular movements brought about by microtubules. These are kinesins and dyneins.
Kinesins and dyneins move in opposite directions. Kinesin are molecules consisting of two heavy and two light chains. The heavy chains have amino terminal globular head responsible for binding to both microtubules and ATP. Hydrolysis of ATP provides the energy needed for movement. The two light chains are responsible for binding to the other cell components, such as organelles and vesicles that are transported along microtubules. Dynein, on the other hand, is a relative larger molecule also composed of heavy and light chains. The same functions are done by these heavy and light chains. These proteins are responsible of moving organelles toward and away the center of the cells. Some play more specific roles, such as repositioning the Golgi apparatus from the center of the cell to that near the centrosome.
Other important motor proteins are actin and myosin. Myosin is considered a prototype of a molecular motor as it is able to convert chemical energy in the form of ATP to mechanical energy. These types of movements can be as complex as the movements in muscle contraction. Interaction between actin and myosin are responsible for muscle contraction, non-muscle movement and even cell division. Cytoskeletons derived from actin are also responsible for the crawling motion of cells on a surface. This movement is brought about by actin polymerization, as well as actin-myosin interaction.
The sliding filament theory explains the possible mechanism in muscle contraction based on the action of myosin and actin. According to this theory, the actin filaments of muscle fibers tend to slide past the myosin filaments during contraction. This was further developed as the cross-bridge model. In the cross-bridge model, actin and myosin form a protein complex called an actomyosin. The head of the myosin attaches itself to the actin filament forming a cross-bridge between them. Contraction occurs when myosin pulls the actin filaments towards the center of the band, then it detaches itself from the actin, and creates a stroke to bind to a next actin molecule.
The correct answers can be found below the references.
1. Which of the following is not a fibrous protein?
2. How many oxygen molecules can one hemoglobin molecule carry?