Server Migration Notice

Starting Aug. 16, 2025 at 9:00 AM (Eastern Standard Time), this server will be shut down temporarily to migrate services to our new server at https://colmar.cloud. Please update your bookmarks accordingly.

All saved user jobs, files, and settings will be migrated automatically. The new server will be fully operational by Aug. 18, 2025.

This current server will remain accessible until Aug. 31, 2025. However, any jobs submitted after Aug. 16, 2025 at 9:00 AM (EST) will NOT be migrated to the new server.

Quantitative model for the binding affinity of intrinsically disordered proteins (IDP) to nano materials: SILC and FRIM models

This web server predicts and plots the binding profile of an intrinsically disordered protein (IDP) in solution to anionic silica nano-particle surface. Optionally, it also allows uploading and display of the experimental binding profile for comparison. The delta_R2 values correspond to the experimentally determined difference of 15N backbone transverse relaxation rates of IDP in presence and absence of the nanoparticles. The delta_R2 values are r elative measures of the interaction strengths of individual residues with the nanoparticles.

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Reference

M. Xie; D.W. Li; J.Q. Yuan and R. Brüschweiler. Dissecting the driving forces for residue-specific binding of intrinsically disordered proteins to nanoparticle surfaces; CHEMISTRY-A EUROPEAN JOURNAL (24) 16997, 2018

D.W. Li; M. Xie and R. Brüschweiler. Quantitative cooperative binding model for intrinsically disordered proteins interacting with nanomaterials; (submitted)

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Acknowledgement

This web server and the research that led to it is supported by the National Science Foundation (Grant No. MCB-0918362)

*This information is only used for the compilation of our webserver usage data.

This server is last updated at September 14 2024 11:34:33.