Research section Research projects and references

Research: ALZHEIMERS Folding Project #18254

Project #18254 overview

Project Summary AI Beta

Alzheimer's disease is marked by clumps of a protein called tau. The project aims to figure out the best computer models to simulate how tau behaves, as these models can help us understand and treat Alzheimer's.
Automated summary; simplified and may not be fully accurate.

Project team

Manager(s)
Justin Miller
Institution
University of Pennsylvania

Work unit

Atoms
302,700
Core
0x26
Status
Public
Source material

Official Project Description

Alzheimer's disease is a significant cause of death and memory loss and there are no effective treatments to halt or reverse disease progression.

One of the late hallmarks and primary biomarkers of Alzheimer's disease is the presence of neurofibrillary tangles, intracellular aggregates of the tau protein.

When behaving properly, tau interacts with microtubules- a critical portion of the cytoskeleton of cells- to help regulate their growth and stability.

However, tau misbehavior and aggregation is also closely linked to Alzheimer's disease among many other neurodegenerative diseases. Studying tau experimentally has been difficult as it is an Intrinsically Disordered Protein (IDP).

As such, traditional structural biology approaches are unable to capture the conformational states of tau in atomistic detail.

Recently, our collaborators have utilized single molecule FRET experiments to experimentally characterize tau by measuring the pairwise distance between different regions.

While simulations of tau could provide atomistic detail of the tau conformational ensemble, historically simulations of IDPs have been challenging as force fields (the parameters which govern the underlying physics of a simulation) and their accompyning models of waters have favored well-folded proteins.

In this project series we embark on an effort to characterize which force field and water models most accurately recapitulate tau experimental results.

We believe these findings will be broadly applicable to all researchers studying intrinsically disordered proteins, and aspire to keep performing these benchmarking simulations as new force field and waters are released.

We also expect these simulations to yield useful information about the tau conformational ensemble. N.B.

because tau is an intrinsically disordered protein, it can fully unfold and refold quite rapidly.

To ensure the protein remains in water the entire simulation, we have included a large number of waters in the system.

As a result these simulations are a good deal more RAM intensive than prior FAH simulations.

Accordingly, we have implemented a minimum system memory requirement of 8000 MiB to run these simulations.

p18251 - amber99sb-disp with tip4pd water.

Performance data

Hardware Performance for Project 18254

Compare community-sampled Folding@Home output for the GPUs and CPUs processing this project.

Data as of Friday, 14 August 2026 15:27:19

GPU PPD Averages

Rank
Project
Model Name
Folding@Home Identifier
Make
Brand
GPU
Model
PPD
Average
Points WU
Average
WUs Day
Average
WU Time
Average
1 Radeon RX 6800/6800XT/6900XT
Navi 21 [Radeon RX 6800/6800XT/6900XT]
AMD Navi 21 5,411,114 67,770 79.85 0 hrs 18 mins
2 RX 5600 OEM/5600XT/5700/5700XT
Navi 10 [RX 5600 OEM/5600XT/5700/5700XT]
AMD Navi 10 1,504,671 67,770 22.20 1 hrs 5 mins