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paw2323 paw2323
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7 years ago
There are 20100 different possible sequence combinations for a protein chain with 100 amino acids. In addition to the amino acid sequence of the protein, what other factors increase the potential for diversity in these macromolecules?
 
  (a) free rotation around single bonds during synthesis
  (b) noncovalent interactions sampled as protein folds
  (c) the directionality of amino acids being added
  (d) the planar nature of the peptide bond
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gracieelaine12gracieelaine12
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Anonymous
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3 months ago
Help! The answer is missing an explanation...
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2 months ago
Quote from: paw2323 (7 years ago)
There are 20100 different possible sequence combinations for a protein chain with 100 amino acids. In addition to the amino acid sequence of the protein, what other factors increase the potential for diversity in these macromolecules?     (a) free rotation around single bonds during synthesis   (b) noncovalent interactions sampled as protein folds   (c) the directionality of amino acids being added   (d) the planar nature of the peptide bond
The correct answer is (b) noncovalent interactions sampled as protein folds**. This is because the way a protein folds and the interactions between its amino acids (like hydrogen bonds, van der Waals forces, and ionic interactions) greatly increase the diversity of possible protein structures, beyond just the sequence of amino acids. The other options, while important, don't add as much diversity in structure as the folding process does.
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