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Folding polypeptide α‐carbon backbones by distance geometry methods
Author(s) -
Aszóadi A.,
Taylor W. R.
Publication year - 1994
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360340406
Subject(s) - monomer , chemistry , folding (dsp implementation) , polar , copolymer , carbon fibers , globular protein , molecule , solvent , protein folding , chain (unit) , hydrophobic effect , chemical physics , crystallography , polymer , organic chemistry , physics , algorithm , computer science , biochemistry , astronomy , composite number , electrical engineering , engineering
Polypeptide α‐carbon backbones were modeled as freely rotating chains made up of spherical monomers. The monomers were assigned an abstract binary “hydrophobicity” property that could be either present or absent. Under the assumption that “hydrophobic” residues tend to cluster together, away from the polar solvent, three‐dimensional conformations of random copolymers of “hydrophobic” and “hydrophilic” monomers were calculated by a novel algorithm based on distance geometry techniques. The simulated molecules were globular and compact, in shape, and possessed distinct hydrophobic cores, indicating that our method was capable of reproducing some of the important global features of real polypeptides. © 1994 John Wiley & Sons, Inc.