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Regensburg 2019 – wissenschaftliches Programm

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CPP: Fachverband Chemische Physik und Polymerphysik

CPP 52: Biomaterials and biopolymers I (joint session BP/CPP)

CPP 52.10: Vortrag

Donnerstag, 4. April 2019, 12:00–12:15, H10

Sequence effects on size, shape, and structural heterogeneity in Intrinsically Disordered Proteins — •Upayan Baul1, Debayan Chakraborty2, Mauro L. Mugnai2, John E. Straub3, Devarajan Thirumalai2, and Joachim Dzubiella11Institute of Physics, Albert-Ludwigs-University of Freiburg, Hermann-Herder-Strasse 3, 79104 Freiburg, Germany — 2Department of Chemistry, The University of Texas at Austin, Austin, Texas 78712 — 3Department of Chemistry, Boston University, Boston, Massachusetts 02215

Intrinsically disordered proteins (IDPs) lack well-defined three-dimensional structures, thus challenging the archetypal notion of structure-function relationships in proteins. We present the development of a coarse grained simulation model that quantitatively characterizes the structural features of IDPs as a function of sequence and length (NT). For diverse IDP sequences, with NT ranging from 24 to 441, our simulations not only reproduce the radii of gyration (Rg) obtained from experiments, but also predict the scattering intensity profiles in near quantitative agreement with Small Angle X-ray Scattering experiments. While Rg values are well-described by the standard Flory scaling law, Rg = R0 NTν, with ν=0.588, analyses reveal that the extent of conformational heterogeneity for IDPs is highly sequence-dependent, even though ensemble-averaged properties suggest synthetic polymer-like behavior in a good solvent. In conclusion, we comment on the effects of external stimuli such as salt concentration and temperature on the conformational properties of polypeptide sequences.

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