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djverab [1.8K]
3 years ago
13

A polypeptide in its native conformation has weak interactions between its R groups. However, when that same polypeptide is dena

tured, these R groups similarly interact with water. Why, then, is the native structure more stable than the denatured one
Chemistry
1 answer:
sasho [114]3 years ago
8 0

Answer:

A protein is more stable in its native form, because apart of weak interactions between R groups, it also presents other stronger interactions, as those including covalent bonds  

Explanation:

For example, covalent bonds between sulfur atoms when disulfide bridges are built.  These links are very difficult to break and maintains the protein shape.  Disulfide bonds are a few but they use to incide in the structure of native proteins

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The  balanced net  equation  for

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Step 1:  <em>write a balanced   molecular equation</em>

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Step 2:   <em>Break all soluble  electrolytes  in to ions</em>

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<em> Ba^2+(aq)  + SO4^2-(aq)→  BaSO4(s</em><em>)</em>

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