title: Proteins as fractals: role of the hydrodynamic interaction.
abstract: Exploiting the fractal nature of folded proteins, we study the effect of the hydrodynamic interaction between amino acids using a Zimm-type model. We compute the time-dependent mean square displacement of an amino acid and the time-dependent autocorrelation function of the distance between two amino acids, and we show that these dynamic quantities evolve anomalously, similar to the Rouse-type behavior, yet with modified dynamic exponents. Good agreement is found with recent neutron spin-echo studies of myoglobin and hemoglobin.
authors.affiliation: Stella and Avram Goren-Goldstein Department of Biotechnology Engineering and Ilse Katz Institute for Meso and Nanoscale Science and Technology, Ben-Gurion University of The Negev, Beer Sheva 84105, Israel.
authors.forename: Rony
authors.initials: R
authors.lastname: Granek
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D003198:Computer Simulation; D017709:Fractals; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D014867:Water / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D011506:Proteins; D014867:Water