Reinterpretation of GCN4-p1 folding kinetics: partial helix formation precedes dimerization in coiled coil folding.
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.
Myers
J K
JK
Department of Biochemistry, Duke University Medical Center, Durham, Box 3711, USA.
Oas
T G
TG
D000409:Alanine; D000465:Algorithms; D019943:Amino Acid Substitution; D004268:DNA-Binding Proteins / Q000737:chemistry; D019281:Dimerization; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D005998:Glycine; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D017510:Protein Folding; D011494:Protein Kinases / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D013816:Thermodynamics
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D011494:Protein Kinases; D000409:Alanine; D005998:Glycine