ProjectANR-2 – Dynamik, Kinetik und Ag-gregation in Modellsystemen intrinsisch ungeordneter
Basic data
Acronym:
ANR-2
Title:
Dynamik, Kinetik und Ag-gregation in Modellsystemen intrinsisch ungeordneter
Duration:
01/11/2022 to 31/10/2025
Abstract / short description:
This project takes a physical approach to investigate intrinsically disordered proteins (IDPs) in aqueous solutions. Novel X-ray and neutron scattering methods and coarse-grained modeling have been established as suitable techniques to explore IDPs, but systematic studies are still missing to combine these methods into a general, comprehensive description of IDPs.
Therefore, the objectives of this project are to use scattering techniques combined with modeling and simulations
(1) to characterize the conformations sampled by model IDPs under different well-controlled conditions,
(2) to analyze how these conformations depend on the chemical properties of the IDPs, and
(3) to understand how and why small differences in chemical properties and conformations lead
to large differences in self-assembly pathways for IDPs.
To this effect, robust, representative model IDP systems will be employed and be compared to natively folded protein reference systems.
These objectives shall help to contribute to answer the central guiding question of the project:
How does disorder of proteins affect their assembly and the associated dynamics from the amino acid level up to the length scale of protein assemblies?
The central guiding question will be addressed by a series of more fundamental questions that will each give rise to a work package (WP) in this project.
The answers to these questions shall help to test the central hypothesis that differences in protein disorder govern the behavior on all length scales from the segmental dynamics to the macroscopic aggregation and phase behavior.
Therefore, the objectives of this project are to use scattering techniques combined with modeling and simulations
(1) to characterize the conformations sampled by model IDPs under different well-controlled conditions,
(2) to analyze how these conformations depend on the chemical properties of the IDPs, and
(3) to understand how and why small differences in chemical properties and conformations lead
to large differences in self-assembly pathways for IDPs.
To this effect, robust, representative model IDP systems will be employed and be compared to natively folded protein reference systems.
These objectives shall help to contribute to answer the central guiding question of the project:
How does disorder of proteins affect their assembly and the associated dynamics from the amino acid level up to the length scale of protein assemblies?
The central guiding question will be addressed by a series of more fundamental questions that will each give rise to a work package (WP) in this project.
The answers to these questions shall help to test the central hypothesis that differences in protein disorder govern the behavior on all length scales from the segmental dynamics to the macroscopic aggregation and phase behavior.
Involved staff
Managers
Faculty of Science
University of Tübingen
University of Tübingen
Institute of Applied Physics (IAP)
Department of Physics, Faculty of Science
Department of Physics, Faculty of Science
Other staff
Institute of Applied Physics (IAP)
Department of Physics, Faculty of Science
Department of Physics, Faculty of Science
Institute of Applied Physics (IAP)
Department of Physics, Faculty of Science
Department of Physics, Faculty of Science
Local organizational units
Institute of Applied Physics (IAP)
Department of Physics
Faculty of Science
Faculty of Science
Funders
Bonn, Nordrhein-Westfalen, Germany