Journal article Open Access

Mass fractal dimension and the compactness of proteins

Enright, Matthew B.; Leitner, David M.

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        <foaf:name>Enright, Matthew B.</foaf:name>
        <foaf:givenName>Matthew B.</foaf:givenName>
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        <foaf:name>Leitner, David M.</foaf:name>
        <foaf:givenName>David M.</foaf:givenName>
    <dct:title>Mass fractal dimension and the compactness of proteins</dct:title>
    <dct:issued rdf:datatype="">2005</dct:issued>
    <dct:issued rdf:datatype="">2005-01-27</dct:issued>
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    <dct:description>Vibrational dynamics and energy flow in a protein are related by Alexander-Orbach theory to the protein's mass fractal dimension, D, and spectral dimension, d . Burioni et al. [Proteins: Struct., Funct. and Bioinformatics 55, 529 (2004)] recently proposed a relation between d and protein size based on their computational analysis of a set of proteins ranging from about 100 to several thousand amino acids. We report here values for D computed for 200 proteins from the Protein Data Bank (PDB) ranging from about 100 to over 10,000 amino acids and examine variation of D with protein size. The average D is found to be 2.5, significantly smaller than a completely compact 3- dimensional collapsed polymer. Indeed, we find that on average a protein in its PDB configuration fills about three-quarters of the volume within the protein surface. Protein mass is also found to scale with radius of gyration with an exponent of 2.5 for this set of proteins.</dct:description>
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