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Related Experiment Video

Updated: Apr 3, 2026

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

The HADDOCK2.2 Web Server: User-Friendly Integrative Modeling of Biomolecular Complexes.

G C P van Zundert¹, J P G L M Rodrigues¹, M Trellet²

¹Bijvoet Center for Biomolecular Research, Faculty of Science Department of Chemistry, Utrecht University, Domplein 29, 3512 JE Utrecht, the Netherlands.

Journal of Molecular Biology

|September 28, 2015

Summary

This summary is machine-generated.

The HADDOCK2.2 portal enhances biomolecular complex structure prediction by integrating more data. This updated tool offers improved protocols and features for researchers in structural biology and drug design.

Keywords:

biomolecular docking data-driven grid computing hybrid modeling protein complexes

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Published on: December 25, 2021

Area of Science:

Structural biology
Computational chemistry
Drug design

Background:

Accurate prediction of quaternary structure is crucial for understanding cellular mechanisms and developing new drugs.
Integrative structural biology methods improve modeling accuracy by incorporating diverse experimental and predictive data.
The HADDOCK (High Ambiguity Driven DOCKing) approach utilizes information-driven strategies for biomolecular complex modeling.

Purpose of the Study:

To present the updated HADDOCK2.2 portal, enhancing its capabilities for predicting biomolecular complex structures.
To introduce new features, improved protocols, and a user-friendly interface for the HADDOCK web server.
To support the scientific community in addressing complex biological questions through advanced structural modeling.

Main Methods:

Information-driven docking approach (HADDOCK).
Integration of experimental and predictive data into modeling protocols.
Development of an updated web portal (HADDOCK2.2) with enhanced features and user interface.

Main Results:

HADDOCK2.2 offers support for mixed molecule types and additional experimental restraints.
Improved protocols and a user-friendly interface enhance the usability of the web server.
The HADDOCK portal has a large user base (over 6000 registered users) and has served over 108,000 jobs.

Conclusions:

The HADDOCK2.2 upgrade provides advanced tools for biomolecular structure prediction.
The enhanced portal facilitates the integration of diverse data for more accurate modeling.
This resource aims to accelerate discoveries in structural biology and drug design.