Sandbox Reserved 197: Difference between revisions

One particular feature of RNase A is the presence of ''cis'' proline residues.  In nature, most amino acids reside in a ''trans'' conformation. Due to their cyclic structure, prolines are more stable in a ''cis'' conformation. RNase A contains four proline residues, two reside in the ''cis'' conformation and two in the ''trans'' conformation. The <scene name='Sandbox_Reserved_197/Tyr92-pro93/5'>Tyr92-Pro93</scene> peptide group of RNase A in its native state is found in the ''cis'' conformation. Despite a <scene name='Sandbox_Reserved_197/P93a/7'>P93A</scene> mutation, a ''cis'' conformation still forms; this is an unlikely conformation for an alanine residue.  Upon unfolding, Tyr92-Ala93 undergoes isomerization to form its favored ''trans'' conformation. This points to the fact that this ''cis'' bond formation is a key component to the protein structure of RNase A.  

<scene name='Sandbox_Reserved_197/P114g/1'>P114G</scene>