What happens to protein structure at low and high pH?

Answer 1

A change in PH can alter the 3D confirmation of the protein cauzing it to lose function partially or completely.

**** A change in pH can denature a protein and also can cause it to change shape, therefore making it useless****

Answer 2

They begin to "denature" or decompose to a certain extent. This breaking down of the protein structure cause it to lose shape. It also restricts it from functioning properly and often interferes with other protein processes.

Answer 3

Depending on the type of protein, some proteins become denatured when exposed to harsh PH levels, such as high or low. Once the protein is denatured it will no longer be able to perform its task as well, if at all.

Hope this helped :)

Answer 4

A drastic change in pH, temperature, or salt concentration can change the tertiary level, which leads to the denaturing of the protein. Sometimes, when the pH, temperature, or salt concentration is restored, the protein can renature, but doesn't always happen. This is one of the reason why dwelling in an area with extreme temperature can be harmful.

Answer 5

At high temperatures, proteins generally denature, or unfold, which means they lose there overall structure necessary for proper function. Every protein has a particular ideal temperature at which its activity is maximized.

At low but non-freezing temperatures, proteins become more stable. Less thermal energy in the system means that the proteins spatial fluctuations will decrease. However, this often results in decreased activity of the protein.

At freezing temperatures, proteins generally lose their native conformation as they interact with rigid ice crystals.

Answer 6

At low pH, proteins can denature due to disruption of hydrogen bonds, resulting in loss of their functional shape and activity. At high pH, proteins can also denature due to changes in ionization of amino acid residues, leading to loss of structure and function. Both low and high pH extremes can disrupt the delicate balance of interactions that maintain protein structure.