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Figure 1. | |||
Proline and Glycine Rich Sequences Adopt Polyproline II Helices | |||
A. Polyproline peptides adopt isolated polyproline II helices in aqueous solution. | |||
B. Substituting every third proline residue (black) for glycine (green) allows three chains to associate to form triple polyproline II helical structure of collagen. | |||
C. Swapping of additional prolines by glycine permits proteins with two layers of polyproline II helices to form, such as snow flea antifreeze proteins. | |||
D. Substitution of all proline residues (shown in black) by glycine (colored green) gives rise to a multilayered “honeycomb” of polyproline II helices, such as that seen in peptides composed of just glycine 53 and Human Anaplastic Leukemia Kinase64. | |||
Latest revision as of 06:01, 14 August 2025
Figure 1. Proline and Glycine Rich Sequences Adopt Polyproline II Helices
A. Polyproline peptides adopt isolated polyproline II helices in aqueous solution.
B. Substituting every third proline residue (black) for glycine (green) allows three chains to associate to form triple polyproline II helical structure of collagen.
C. Swapping of additional prolines by glycine permits proteins with two layers of polyproline II helices to form, such as snow flea antifreeze proteins.
D. Substitution of all proline residues (shown in black) by glycine (colored green) gives rise to a multilayered “honeycomb” of polyproline II helices, such as that seen in peptides composed of just glycine 53 and Human Anaplastic Leukemia Kinase64.
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