Answer
Protein is a complex biomolecule with a long stretch of amino acids joined by a peptide bond. A protein is usually more than 100 amino acids long below that number they are called polypeptides, for example, insulin is 51 amino acids long and is a polypeptide. The smallest peptide is glutathione with only three amino acids. Proteins are synthesized based on the information present in the DNA in the cells and the linear structure synthesized is called primary structure and these are further folded in the cytoplasm by various other molecules known chaperones forming the secondary, tertiary and quaternary structures. Protein, in its native state, it is fully formed and functional. During this state, it may be folded and other interactions between the atoms such as sulphide bridges, hydrogen bonding and non-covalent interactions are observed. These bonds help the protein to be stable by placing the hydrophobic or water-hating amino acids at its core and hydrophilic amino acids at the periphery. The sulphide bridges fix the coiled state of the protein. The amino acids directly involved in the function such as cleavage of molecules, bonding might be far from each other in the primary/ linear sequence of the protein but the folding of the protein helps them orient them and this site in the enzymes is called the active site. In a folded state the protein is well protected from the physical damages. Hence, for a long polypeptide of above 100 amino acids, it is highly unlikely that a protein exists in an irregular during its native state. But, the denaturing agents such as acids, heat etc can damage the protein structure.
Work Step by Step
Protein is a complex biomolecule with a long stretch of amino acids joined by a peptide bond. A protein is usually more than 100 amino acids long below that number they are called polypeptides, for example, insulin is 51 amino acids long and is a polypeptide. The smallest peptide is glutathione with only three amino acids. Proteins are synthesized based on the information present in the DNA in the cells and the linear structure synthesized is called primary structure and these are further folded in the cytoplasm by various other molecules known chaperones forming the secondary, tertiary and quaternary structures. Protein, in its native state, it is fully formed and functional. During this state, it may be folded and other interactions between the atoms such as sulphide bridges, hydrogen bonding and non-covalent interactions are observed. These bonds help the protein to be stable by placing the hydrophobic or water-hating amino acids at its core and hydrophilic amino acids at the periphery. The sulphide bridges fix the coiled state of the protein. The amino acids directly involved in the function such as cleavage of molecules, bonding might be far from each other in the primary/ linear sequence of the protein but the folding of the protein helps them orient them and this site in the enzymes is called the active site. In a folded state the protein is well protected from the physical damages. Hence, for a long polypeptide of above 100 amino acids, it is highly unlikely that a protein exists in an irregular during its native state. But, the denaturing agents such as acids, heat etc can damage the protein structure.
