Protein Structure and Functions - Biochemistry

Heme normally binds to iron. Myoglobin is mostly concentrated in muscles, and after a muscle injury can be present in blood. Myoglobin has a higher affinity for oxygen than hemoglobin; myoglobin’s oxygen saturation curve is hyperbolic, whereas hemoglobin’s is sigmoidal. Hemoglobin F (fetal hemoglobin) has a higher oxygen affinity than hemoglobin A (adult hemoglobin). This improves the transfer of oxygen from the circulation of the mother to that of the fetus.

Chymotrypsin is a digestive enzyme that breaks down proteins (proteolysis). It has a catalytic triad of serine, histidine, and aspartate. The hydroxyl group on serine acts as a nucleophile and attacks the carbonyl group on the amino acid, forming a tetrahedral intermediate. Histidine acts as a base, which cleaves the peptide bond. Aspartate acts as an acid, which restores the active site. Since this catalytic triad has a defined nucleophile, base, and acid, we know that there will not be an additional thiol nucleophile. Thiol nucleophiles are found in cysteine proteases.

Actin filaments, also known as microfilaments, are flexible and bundle up, and are 5-9nm in diameter. Intermediate filaments, which can strengthen cells, are about 10nm. Microtubules, rigid and attached on one end to a centrosome, are 25nm.

The primary structure of a protein is defined by the sequence of amino acid residues. It is this sequence that lays the foundation for all other higher levels of structures in a protein. Secondary structure is defined by the hydrogen bonding between the carboxyl and amino backbone of the amino acids. Tertiary is defined by amino acid side chain interactions. Finally, quaternary structure is defined by the assembly of subunits of a protein into the overall larger protein structure.

The primary structure is only composed of the sequence of amino acids in a protein. The secondary structure is the alpha or beta folding that occurs due to amino acid interaction. The tertiary structure is the three dimensional folding that occurs within a protein. Finally, quaternary structure occurs when a protein has two or more polypeptide sub-units. A perfect example of quaternary structure is found in hemoglobin.

The formation of a peptide bond is an example of a condensation reaction. This is because, when two amino acids come together, a water molecule is let go.

Because an amino acid has been altered in sickle cell anemia, we can say that the amino acid sequence for hemoglobin has been changed. The amino acid sequence is defined as the primary structure for a protein, so that is the level that has been altered. It should be noted that the subsequent levels of protein structure would be altered as well, but the manipulation of the amino acid sequence is a changing of the primary structure first.

Hemoglobin is the only available example of a macromolecule composed of multiple subunits. Hemoglobin has frou subunits, each capable of binding and transporting one molecule of oxygen in the blood.

Chymotrypsin and myogblobin are both simple proteins, each consisting of a single polypeptide. These proteins do not have multiple subunits; thus their highest level of structure is tertiary (three-dimensional). Lactose and sucrose are disaccharides, each composed of two carbohydrate monomers (monosaccharides).

Hemoglobin is a tetramer that possesses a quaternary structure containing multiple folded polypeptide structures (tertiary structures). A tertiary protein will commonly contain a single polypeptide chain with one or more secondary structures.

A protein with multiple identical subunits does indeed have a quaternary structure; in these cases, dimers and tetramers are common. The main forces holding together oligomeric subunits are weak, non-covalent interactions, specifically, hydrophobic ones, as well as electrostatic forces. Subunits do not necessarily form separate domains within a protein; in a potassium channel protein, for example, there are identical subunits which come together to form the single channel. Proteins’ 3D-structures do indeed sometimes change when ligands bind; this change help regulate the proteins’ biological activity.

Quaternary structure of a protein involves the assembly of subunits. Hemoglobin, p53 and DNA polymerase are all composed of subunits, while myoglobin is a functional single sequence. Since myoglobin does not have multiple subunits, it does not have quaternary structure.

Quaternary structure describes how polypeptide chains fit together to form a complete protein. Quaternary protein structure is held together by hydrophobic interactions, and disulfide bridges. The sequence of amino acids is known as primary structure; helices, sheets, and similar features are part of the secondary structure; and the 3-D organization is tertiary structure. "The four parts of a protein's amino acid sequence" does not refer to anything in particular.

Primary structure: linear sequence of amino acids

Secondary structure: hydrogen bonds, alpha-helices and beta-pleated sheets

Tertiary structure: disulfide bonds, single polypeptide chain

Myoglobin is a monomer, and is made of a single polypeptide chain. Thus, its highest level of protein structure is tertiary. While collagen does contain different polypeptide chains, it is an example of a protein with quaternary structure, not an explanation of what this means.

While covalent bonds create the primary structure of a protein, and hydrogen bonding and Van der Waals forces have a large impact on the secondary structure of a protein, they are not the main contributors to overall folding of a protein. This has more to do with solvation costs, hydrophobicity, and entropy. The hydrophobicity and hydrophobic portions of the protein must fold to minimize entropic costs.

Hemoglobin is a classic example of protein with a quaternary structure. The binding of oxygen to one sub unit increases the affinity of the other sub units for oxygen (cooperativity). Adult hemoglobin is made of two alpha globin and two beta globin polypeptides. Protein quaternary structure may involve both noncovalent and covalent forces.

Hydrogen bonds stabilize interactions among the amide and carboxyl groups in the main chain of the polypeptide. These interactions may induce the formation of alpha-helices and/or beta-pleated sheets.

Alpha helices and beta sheet, the dominant secondary structural motifs in polypeptides are formed by hydrogen bonds between the carbonyl and amino groups of the amino acid backbone.

In an antiparallel beta sheet, the hydrogen bonding angle is 180 degrees and optimal; this is the most stable angle. In parallel sheets, it is a less stable 150 degrees. Whether a sheet is parallel or antiparallel does not tell us anything about what amino acids it is composed of, so each of the other answers is incorrect.

In an alpha helix, hydrogen bonding occurs every four amino acids, starting from the 1st binding to the 4th in the sequence; the 2nd amino acid binds to the 6th, the 3rd to the 7th, and so on.

Covalent bonding is when two nonmetals share electrons in order to form a bond. This type of bonding can be observed in the primary (peptide bonds), tertiary (disulfide bonds), and quaternary (disulfide bonds) levels of protein structure. The secondary structure of proteins only uses hydrogen bonding as the folding force.