Native state

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In biochemistry, the native state of a protein or nucleic acid is its properly folded and/or assembled form, which is operative and functional.[1] The native state of a biomolecule may possess all four levels of biomolecular structure, with the secondary through quaternary structure being formed from weak interactions along the covalently-bonded backbone. This is in contrast to the denatured state, in which these weak interactions are disrupted, leading to the loss of these forms of structure and retaining only the biomolecule's primary structure.

Biochemistry

Proteins

While all protein molecules begin as simple unbranched chains of

).

Many

conformation
" or "structure."

Folded and unfolded proteins are often easily distinguished by virtue of their water solubilities, as many proteins become insoluble on denaturation. Proteins in the native state will have defined

nuclear magnetic resonance
(NMR).

The native state of a protein can be distinguished from a

sequence
may touch or lie very close to one another within a stably folded protein. In a molten globule, on the other hand, their time-averaged distances are liable to be greater.

Learning how native state proteins can be manufactured is important, as attempts to create proteins from scratch have resulted in molten globules and not true native state products. Therefore, an understanding of the native state is crucial in protein engineering.

Nucleic acids

Nucleic acids attain their native state through

tRNA often form complex native configurations approaching the complexity of folded proteins. Additionally, artificial nucleic acid structures used in DNA nanotechnology
are designed to have specific native configurations in which multiple nucleic acid strands are assembled into a single complex. In some cases native state of biological DNA performs their functions without being controlled by any other regulatory units.

References