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Related Experiment Video

Updated: May 24, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Published on: June 3, 2014

The FoldX web server: an online force field.

Joost Schymkowitz¹, Jesper Borg, Francois Stricher

¹Switch Laboratory, Flanders Interuniversity Institute for Biotechnology (VIB), Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussel, Belgium. joost.schymkowitz@skynet.be

Nucleic Acids Research

|June 28, 2005

Summary

This summary is machine-generated.

FoldX is a computational tool for predicting how mutations affect protein stability and dynamics. Its core functions, including free energy calculations and alanine scanning, are now accessible via a public web server.

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Area of Science:

Biochemistry
Structural Biology
Computational Biology

Background:

Protein stability and dynamics are crucial for biological function.
Predicting the impact of mutations is essential for understanding disease and protein engineering.
Empirical force fields offer a rapid approach to evaluating these effects.

Purpose of the Study:

To make the core functionality of the FoldX empirical force field publicly available.
To provide a web server for rapid evaluation of mutation effects on protein and nucleic acid stability, folding, and dynamics.
To extend the utility of FoldX for structural and energetic analysis.

Main Methods:

Utilizing the FoldX empirical force field for macromolecule free energy calculations based on 3D structures.
Implementing core FoldX functionalities, including stability calculations, proton positioning, water bridge prediction, metal binding site prediction, and complex formation free energy analysis.
Incorporating alanine scanning and detailed reporting functions for atomic interaction networks and per-residue energetic analysis.

Main Results:

The core FoldX functionality is now accessible via a public web server (http://foldx.embl.de/).
The web server supports calculations of protein stability, proton positions, water bridges, metal binding sites, and complex formation free energy.
New features include alanine scanning, atomic interaction network visualization, and detailed structural/energetic reporting per atom or residue.

Conclusions:

The public release of the FoldX web server democratizes access to powerful tools for analyzing protein and nucleic acid behavior.
This resource facilitates rapid assessment of mutation effects, aiding research in structural biology and protein engineering.
Future extensions of FoldX applications promise further advancements in macromolecular analysis.