Folding of a miniprotein with mixed fold.
Using the 28 residue betabetaalpha protein FSD-EY as a target system, we examine correction terms for the ECEPP/3 force field. We find an increased probability of formation of the native state at low temperatures resulting from a reduced propensity to form alpha helices and increased formation of beta sheets. Our analysis of the observed folding events suggests that the C-terminal helix of FSD-EY is much more stable than the N-terminal beta hairpin and forms first. The hydrophobic groups of the helix provide a template which promotes the formation of the beta hairpin that is never observed to form without the helix.
Mohanty
Sandipan
S
John von Neumann Institut für Computing, Forschungszentrum Jülich, Jülich D-52425, Germany. s.mohanty@fz-juelich.de
Hansmann
U H E
UH
D004268:DNA-Binding Proteins / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics; D014157:Transcription Factors / Q000737:chemistry*
D004268:DNA-Binding Proteins; C108466:FSD-1 protein, synthetic; D014157:Transcription Factors