Research section Research projects and references

Research: ALZHEIMERS Folding Project #18289

Project #18289 overview

Project Summary AI Beta

Alzheimer's disease is caused by abnormal protein clumps called tau tangles. Scientists are using powerful computer simulations to study how tau behaves in water. This project focuses on simulating the entire tau protein to understand how it malfunctions and causes Alzheimer's.
Automated summary; simplified and may not be fully accurate.

Project team

Manager(s)
Justin Miller
Institution
University of Pennsylvania

Work unit

Atoms
7,950,330
Core
0x28
Status
Beta

No related projects listed.

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 accompanying models of waters have favored well-folded proteins.

In project p18251-18264, we looked at a portion of tau (the proline rich region) and sought to compare our results to experimentally observed features of tau (see here - https://foldingathome.org/2026/02/19/force-field-comparisons/).

Now, we aim to simulate the entire protein in the best force field/water model. 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 64Gb to run this project.

Similarly network requirements are significant.

We have attempted to set points accordingly for the increased system usage.

Performance data

Hardware Performance for Project 18289

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

Data as of Sunday, 06 September 2026 12:23:45

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 GeForce RTX 4070 SUPER
AD104 [GeForce RTX 4070 SUPER]
Nvidia AD104 141,789,393 11,205,872 12.65 1 hrs 54 mins