Sandbox Reserved 197: Difference between revisions
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Another important role of proline residues is their involvement in β turns. β turns are 180° turns commonly found in globular proteins to allow for a compact structure by connecting the ends of adjacent antiparallel β sheets [http://en.wikipedia.org/wiki/Beta_sheet]. The turn consists of a sequence of four amino acid residues. The carbonyl of the first amino acid hydrogen bonds with the amino group of the fourth amino acid. Proline is involved in β turns because it is small and flexible and assumes a ''cis'' conformation. In RNase A both Pro93 and Pro114 are involved in β turns. | Another important role of proline residues is their involvement in β turns. β turns are 180° turns commonly found in globular proteins to allow for a compact structure by connecting the ends of adjacent antiparallel β sheets [http://en.wikipedia.org/wiki/Beta_sheet]. The turn consists of a sequence of four amino acid residues. The carbonyl of the first amino acid hydrogen bonds with the amino group of the fourth amino acid. Proline is involved in β turns because it is small and flexible and assumes a ''cis'' conformation. In RNase A both Pro93 and Pro114 are involved in β turns. | ||
<Structure load='7RSA' size='500' frame='true' align='left' caption='Insert caption here' scene='Sandbox_Reserved_197/Rnase_a_wild_type/ | <Structure load='7RSA' size='500' frame='true' align='left' caption='Insert caption here' scene='Sandbox_Reserved_197/Rnase_a_wild_type/6' /> | ||
==='''Disulfide Bonds'''=== | ==='''Disulfide Bonds'''=== | ||
