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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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Answer:

See below

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If you look at Pennsylvania in 2020 as an example, they have 20 electoral votes.  Pennsylvania does not split their votes so all go to just one candidate.  In the measurement of votes, it might show that candidate A got 51% of the votes and candidate B got 49%.  The 20 electoral votes would all go to candidate A and candidate B gets nothing.  Candidate B may have gotten millions of individual votes within the state but that no longer matters.  Candidate A won the state so gets all 20 electoral votes.  If the country went by the individual vote, Candidate B would keep all those votes he got from the 2 or 3 large cities in Pennsylvania.

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