Stability of protein and nucleic acid
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Answer:
Nucleic acid structures are stabilized by non-covalent intramolecular interactions between the bases. All biological processes involving DNA and RNA require these structures to be in the stable and in the appropriate conformation. It is important to know how nucleic acids form their biologically active states and how these active states are stabilized.
Protein stability is the net balance of forces, which determine whether a protein will be its native folded conformation or a denatured (unfolded or extended) state. The net stability of proteins is quite small and is the difference between two large opposing forces. The folded native state of protein structures is stabilized by various atomic/group interactions, such as hydrophobic, electrostatic, hydrogen bonding, van der Waals, and disulphide, and the unfolded state is dominated by entropic and nonentropic free energies. It is something of a paradox, given the apparently very complicated three-dimensional structure of proteins and their rapid spontaneous folding, that their net stability is so small, typically 5–10 kcal/mol .
Answer:
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