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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
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