Consider the following tetrapeptide, written in a sequence according to normal convention, from left to right:       Residue 1 is acidic; Residue 2 is cysteine (an amino acid containing a –CH2SH R-group); Residue 3 is proline (a large hydrophobic amino acid); Residue 4 is basic.    Of the following four general statements, which one is TRUE regarding this tetrapeptide?   This tetrapeptide does not have the ability to form a disulfide linkage with an identical tetrapeptide. Residue 2 belongs to the amino acid category known as "basic." 3 of these 4 responses are correct This tetrapeptide could be part of an alpha-helix, since the large size of the proline would not have any impact on the consistency of the spiral shape. The acidic residue (Residue #1) is at the amino terminus of this tetrapeptide.

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Consider the following tetrapeptide, written in a sequence according to normal convention, from left to right:

      Residue 1 is acidic; Residue 2 is cysteine (an amino acid containing a –CH2SH R-group); Residue 3 is proline (a large hydrophobic amino acid); Residue 4 is basic. 

 

Of the following four general statements, which one is TRUE regarding this tetrapeptide?  

This tetrapeptide does not have the ability to form a disulfide linkage with an identical tetrapeptide.
Residue 2 belongs to the amino acid category known as "basic."
3 of these 4 responses are correct
This tetrapeptide could be part of an alpha-helix, since the large size of the proline would not have any impact on the consistency of the spiral shape.
The acidic residue (Residue #1) is at the amino terminus of this tetrapeptide.
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