Proteins: Coexistence of Stability and Flexibility

Shlomi  Reuveni; Rony Granek; Joseph Klafter

3rd International ICST Conference on Performance Evaluation Methodologies and Tools

Research Article

Proteins: Coexistence of Stability and Flexibility

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@INPROCEEDINGS{10.4108/ICST.VALUETOOLS2008.4241,
    author={Shlomi  Reuveni and Rony Granek and Joseph Klafter},
    title={Proteins: Coexistence of Stability and Flexibility},
    proceedings={3rd International ICST Conference on Performance Evaluation Methodologies and Tools},
    publisher={ICST},
    proceedings_a={VALUETOOLS},
    year={2010},
    month={5},
    keywords={},
    doi={10.4108/ICST.VALUETOOLS2008.4241}
}

Shlomi Reuveni
Rony Granek
Joseph Klafter
Year: 2010
Proteins: Coexistence of Stability and Flexibility
VALUETOOLS
ICST
DOI: 10.4108/ICST.VALUETOOLS2008.4241

Shlomi Reuveni¹, Rony Granek², Joseph Klafter¹

1: School of Chemistry, Tel-Aviv University, Tel-Aviv 69978, Israel
2: Department of Biotechnology Engineering, Ben-Gurion University, Beer Sheva 84105, Israel

Abstract

We introduce an equation for protein native topology based on recent analysis of data from the Protein Data Bank and on a generalization of the Landau-Peierls instability criterion for fractals. The equation relates the protein fractal dimension df, the spectral dimension ds, and the number of amino acids N. Deviations from the equation may render a protein unfolded. The fractal nature of proteins is shown to bridge their seemingly conflicting properties of stability and flexibility. Over 500 proteins have been analyzed (df, ds, and N) and found to obey this equation of state.

Published: 2010-05-16
Publisher: ICST
Modified: 2010-05-16

: http://dx.doi.org/10.4108/ICST.VALUETOOLS2008.4241