In: Biology
Topic: Protein Denaturation
1) What are the various levels of organization that any protein structure may have that gives it its 3D shape? Which of these changes during denaturation?
2) For each change made to a protein solution, how might it affect the interactions that are involved in a protein's shape?
3) What is the difference between precipitation of a protein and its denaturation? How might you tell the difference?
1.
Proteins are a class of macromolecules which are built from amino acids. They exhibit 4 levels of organization, namel -
Primary structure: it just represents the amino acid sequence of a protein.
Secondar structure: refers to the local spatial arrangement of the main chain atoms of a swgment of polypeptide.
Tertiary structure: it represents the 3D structure of a polypeptide chain.
Quarternary structure: represnts the arrangement of the subunits of a protein.
Ionic bonds, H bonds, hydrophobic interactions, covalent bonds.
The peptide bond is an amide bond formed between the amino and carboxyl group of two amino acids. Its rigid, planar and has a partial double bond character. Although,
The structure of a protein which is found naturally in a cell is called the native state. This native state gets denatured under extreme conditions like increase/ decrease in pH, high temperature, change in polarity.
Upon denaturation, secondary, tertiary, quarternary structure gets denatured while only the primary structure remains.
Some of the denaturing agents are urea, guanidinium chloride, etc.