Let’s get acquainted with its meaning. A protein itself has a lot of things in it. Protein containing more than one polypeptide shows quaternary structure.
Quaternary Structure
Quaternary structure is the arrangement of multiple polypeptide chains in a protein. For example, hemoglobin contains two alpha chains and two beta chains that are held together by noncovalent interactions. Certain enzymes have subunits with different functions, each of which contributes to the overall function of the enzyme.
A protein containing more than one polypeptide chain exhibits quaternary structure. Quaternary structure is the arrangement of subunits within a larger complex. It is in contrast to the secondary and tertiary structures of a protein, which are the folding patterns of single polypeptide chains.
A single polypeptide chain can fold into numerous different conformations, but these are all dependent on interactions between residues in the primary sequence of the chain and mainly involve hydrogen bonds. This is known as an alpha-helix or beta-sheet conformation.
This differs from quaternary structure, where several different polypeptide chains are involved in intermolecular interaction. The pattern formed by those interactions is not limited to that of an alpha helix or beta sheet.
Three Dimensional Shape
The three-dimensional shape of a protein is determined by the organization of its polypeptide chains. The shape is dependent on the secondary and tertiary structure of the protein, which describes the locations of alpha helices and beta sheets in relation to each other.
The three-dimensional shape of a protein is the most important factor in determining its function.
Protein structure can be defined by two factors: secondary structure and tertiary structure.
A protein containing more than one polypeptide chain exhibits the phenomenon known as the “secondary structure.” The secondary structure of a polypeptide is any arrangement of hydrogen bonds between the amide groups and carbonyl groups in the polypeptide backbone.
Primary Structure
The term polypeptide is used to refer to a protein that contains more than one polypeptide chain. A polypeptide is a chain of amino acids linked by peptide bonds. A polypeptide can be either linear or branched. The number of amino acids in each polypeptide chain ranges from just a few to several hundred.
The term polypeptide is used to refer to a protein that contains more than one polypeptide chain. A polypeptide is a chain of amino acids linked by peptide bonds. A polypeptide can be either linear or branched. The number of amino acids in each polypeptide chain ranges from just a few to several hundred.
Secondary Structure
Proteins are made up of one or more polypeptide chains that exhibit a variety of possible structures, depending on their amino acid sequences. These structures are characterized as to whether they are alpha helixes, beta sheets, and random coils.
The secondary structure is the most commonly observed and is determined by the hydrogen bonds formed between different regions of the polypeptide chains.
Proteins, which are polymers of amino acids, can sometimes be described in terms of the structure of the polypeptide chain. A protein containing more than one polypeptide chain is known as a multi-subunit protein, and it can be predicted to form alpha helixes or beta sheets after being denatured by heat or acid.
Protein Denaturing
A protein containing more than one polypeptide chain is said to have an aggregate structure. In this structure, the polypeptide chains are denatured so that they are no longer able to assume their normal, native conformation. This denaturing can be caused by manipulation of any of the conditions that affect hydrophobic and electrostatic interactions.
If protein aggregation occurs in vivo, the entire process can lead to disease or cell death. Aggregation may occur because of mutations within the proteins that alter hydrogen bonding and van der Waals forces or because of changes in external conditions such as pH.
The formation of aggregates may also serve a purpose, as in the case with amyloidosis, which is characterized by the extracellular accumulation of polymeric fibrils formed from abnormal insoluble fibers composed mainly of cross-beta (β) sheet structures with amyloid-like cores. These aggregates are associated with many human diseases, including Alzheimer’s disease, type II diabetes and various immune system disorders.
Last words
A protein containing more than one polypeptide chain exhibits quaternary structure—meaning that it is held together by non-covalent bonds and when the protein is in solution, its subunit molecules are distributed in clusters due to hydrogen bonding.