Display Settings:


Send to:

Choose Destination
See comment in PubMed Commons below
Protein Sci. 2011 May;20(5):818-26. doi: 10.1002/pro.605. Epub 2011 Mar 30.

Relative stability of de novo four-helix bundle proteins: insights from coarse grained molecular simulations.

Author information

  • 1Department of Chemistry and Biochemistry and Department of Physics, University of California Santa Barbara, Santa Barbara, California 93106, USA. gbellesia@lanl.gov


We use a recently developed coarse-grained computational model to investigate the relative stability of two different sets of de novo designed four-helix bundle proteins. Our simulations suggest a possible explanation for the experimentally observed increase in stability of the four-helix bundles with increasing sequence length. In details, we show that both short subsequences composed only by polar residues and additional nonpolar residues inserted, via different point mutations in ad hoc positions, seem to play a significant role in stabilizing the four-helix bundle conformation in the longer sequences. Finally, we propose an additional mutation that rescues a short amino acid sequence that would otherwise adopt a compact misfolded state. Our work suggests that simple computational models can be used as a complementary tool in the design process of de novo proteins.

Copyright © 2011 The Protein Society.

[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for John Wiley & Sons, Inc. Icon for PubMed Central
    Loading ...
    Write to the Help Desk