Journal article Open Access

# Mass fractal dimension and the compactness of proteins

Enright, Matthew B.; Leitner, David M.

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<dc:creator>Enright, Matthew B.</dc:creator>
<dc:creator>Leitner, David M.</dc:creator>
<dc:date>2005-01-27</dc:date>
<dc: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.</dc:description>
<dc:identifier>https://zenodo.org/record/895378</dc:identifier>
<dc:identifier>10.1103/physreve.71.011912</dc:identifier>
<dc:identifier>oai:zenodo.org:895378</dc:identifier>
<dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
<dc:title>Mass fractal dimension and the compactness of proteins</dc:title>
<dc:type>info:eu-repo/semantics/article</dc:type>
<dc:type>publication-article</dc:type>
</oai_dc:dc>

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