Reinterpretation of GCN4-p1 folding kinetics: partial helix formation precedes dimerization in coiled coil folding.

Journal Article

The folding of coiled coil peptides has traditionally been interpreted in terms of native dimer and unfolded monomers. Calculations using AGADIR and experimental studies of fragments suggest that the monomers of the coiled coil peptide, GCN4-p1, contain significant residual helical structure. A simple model based on diffusion-collision theory predicts not only the measured folding rate within an order of magnitude, but also predicts remarkably well the effect of alanine to glyXcine mutations. We suggest that intrinsic helix stability is a major determinant of the folding rate of the GCN4 coiled coil.

Full Text

Duke Authors

Cited Authors

  • Myers, JK; Oas, TG

Published Date

  • June 4, 1999

Published In

Volume / Issue

  • 289 / 2

Start / End Page

  • 205 - 209

PubMed ID

  • 10366499

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1006/jmbi.1999.2747

Language

  • eng

Conference Location

  • England