Research section Research projects and references

Research: ALZHEIMERS Folding Project #18252

Project #18252 overview

Project Summary AI Beta

Alzheimer's disease is caused by tangled proteins called tau. Studying these tangles is hard because they don't have a fixed shape. This project will test different computer models to see which one best simulates how tau behaves, helping us understand Alzheimer's better.
Automated summary; simplified and may not be fully accurate.

Project team

Manager(s)
Justin Miller
Institution
University of Pennsylvania

Work unit

Atoms
1,224,788
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 18252

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

Data as of Sunday, 02 August 2026 21:52:55

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 4080 SUPER
AD103 [GeForce RTX 4080 SUPER]
Nvidia AD103 32,890,720 986,037 33.36 0 hrs 43 mins
2 GeForce RTX 3090 Ti
GA102 [GeForce RTX 3090 Ti]
Nvidia GA102 15,764,801 118,000 133.60 0 hrs 11 mins
3 GeForce RTX 4060 Ti
AD106 [GeForce RTX 4060 Ti]
Nvidia AD106 9,425,296 781,033 12.07 1 hrs 59 mins
4 GeForce RTX 4060 Ti 16GB
AD106 [GeForce RTX 4060 Ti 16GB]
Nvidia AD106 9,054,681 758,759 11.93 2 hrs 1 mins
5 GeForce RTX 3060 Ti Lite Hash Rate
GA104 [GeForce RTX 3060 Ti Lite Hash Rate]
Nvidia GA104 7,724,053 731,601 10.56 2 hrs 16 mins
6 Radeon RX 6800/6800XT/6900XT
Navi 21 [Radeon RX 6800/6800XT/6900XT]
AMD Navi 21 4,471,442 118,000 37.89 0 hrs 38 mins
7 GeForce RTX 2060
TU104 [GeForce RTX 2060]
Nvidia TU104 3,190,526 560,133 5.70 4 hrs 13 mins