Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library.

@article{Jha2005HelixSA,
  title={Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library.},
  author={Abhishek K Jha and Andr{\'e}s Colubri and Muhammad H. Zaman and Shohei Koide and Tobin R. Sosnick and Karl F. Freed},
  journal={Biochemistry},
  year={2005},
  volume={44 28},
  pages={9691-702}
}
A central issue in protein folding is the degree to which each residue's backbone conformational preferences stabilize the native state. We have studied the conformational preferences of each amino acid when the amino acid is not constrained to be in a regular secondary structure. In this large but highly restricted coil library, the backbone preferentially adopts dihedral angles consistent with the polyproline II conformation rather than alpha or beta conformations. The preference for the… CONTINUE READING