Available algorithms


A method of calculating secondary structures populations of proteins from their chemical shifts.


A method the prediction of protein secondary structure populations from the amino acid sequence,  which predicts simultaneously structure and intrinsic disorder. It includes polyproline-II prediction. (paper)


A method of rational design of protein variants with enhanced solubility, which includes a prediction of protein solubility scores and solubility profiles (more info).


A sequence-based method of predicting aggregation propensities of proteins.


A method of calculating random coil chemical shifts from protein sequences.


A method of determining protein structures using chemical shifts.


A method of calculating side-chain methyl chemical shifts from protein structures.


A method of calculating side-chain aromatic chemical shifts from protein structures.


A general purpose code for molecular simulations.

For security and privacy reasons we require users to log in to use our software.

Registration is free and takes no time. 





Terms and Conditions

This web-server and its associated data and services are for research purpose only, not for clinical or commercial use. It is a non-profit service to the scientific community. The responsibility of the Vendruscolo research lab is limited to applying best efforts in providing and publishing good programs and data. The University of Cambridge has no responsibility for the use of results, data, or information, which have been provided through this web-server.