If it is accepted that the information for how a protein is intended to fold lies within its primary sequence, explain why a purified protein denatured in vitro might not be able to renature accurately.

Denaturation and renaturation are properties of protein but in some cases denaturation is irreversible and protein is unable to renature.

The primary sequence of a protein determines which portion of protein fold closely together in order to form three-dimensional conformation and the conformations are held by hydrogen bonds.

Denaturation of protein in-vitro is generally obtained by increasing temperature. Heat or high temperature disrupts hydrogen bonds that held between protein folds because high temperature increases the kinetic energy and the bonds are disrupted due to rapid heating. Disruption of hydrogen bonds will change the 3D structure of the protein and denatured proteins lose its function.

Chemicals are also used to disrupt hydrogen bonds such as alcohol.

So, high temperature and chemicals denature protein by affecting the hydrogen bonds holding 3D shape of primary sequence in protein and the change in protein becomes irreversible.

answer: - few nutrients

high pressure

low temperatures

explanation: 1. few nutrients:   open-ocean zone is located way far from the land, which is the main source of the essential nutrients.2. high pressure: pressure increases by 1 atmosphere for every 10 meters increase in depth.3. ample sunlight: a large fraction of the sunlight is reflected back to the atmosphere from the sea surface. 4. varying salinity: below the thermocline, the water is isolated from the atmosphere so the salinity remains stable over the year.5. low temperatures:   the temperature of open-ocean zone ranges from a low of -2°c to an average of 17°c

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explanation: