A breakdown of symmetry in the folding transition state of protein L.

@article{Kim2000ABO,
  title={A breakdown of symmetry in the folding transition state of protein L.},
  author={Daniel E. Kim and Christopher Fisher and David Baker},
  journal={Journal of molecular biology},
  year={2000},
  volume={298 5},
  pages={971-84}
}
The 62 residue IgG binding domain of protein L consists of a central alpha-helix packed on a four-stranded beta-sheet formed by N and C-terminal beta-hairpins. The overall topology of the protein is quite symmetric: the beta-hairpins have similar lengths and make very similar interactions with the central helix. Characterization of the effects of 70 point mutations distributed throughout the protein on the kinetics of folding and unfolding reveals that this symmetry is completely broken during… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 76 extracted citations

Protein Engineering Study of Protein L by Simulation

Journal of Computational Biology • 2002
View 18 Excerpts
Highly Influenced

Intermediates and the folding of proteins L and G.

Protein science : a publication of the Protein Society • 2004
View 7 Excerpts
Highly Influenced

The origins of asymmetry in the folding transition states of protein L and protein G.

Protein science : a publication of the Protein Society • 2002
View 4 Excerpts
Highly Influenced

References

Publications referenced by this paper.
Showing 1-10 of 39 references

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

P. J. Kraulis
J. Appl. Crystallog • 1991
View 4 Excerpts
Highly Influenced

Matching theory and experiment in protein folding.

Current opinion in structural biology • 1999
View 3 Excerpts

Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G.

Proceedings of the National Academy of Sciences of the United States of America • 1999

Robustness of protein folding kinetics to surface hydrophobic substitutions.

Protein science : a publication of the Protein Society • 1999
View 2 Excerpts

Similar Papers

Loading similar papers…