For "Single Protein" searches, we recommend that you upgrade to ProSight Lite.ProSight Lite is a free Windows application for matching a single candidate protein sequence and its modifications against a set of mass spectrometric observations. Thanks, ProSightPTM2 Team |
Users are welcome to use the "guest" account (password "anonymous") but they should be aware that all analyses on this account are removed each night. Further, all results are visible to other users.
This year, at the 62nd ASMS meeting in Baltimore, MD, we released ProSight Lite, a free Windows application for matching a single candidate sequence and its modifications against a set of mass spectrometric observations.
In 2014, we have released three papers on top down proteome informatics.
ProSight PTM 2.0 allows identification and characterization of both intact proteins and peptides. Our PTM Warehouses are annotated with all known post-translational modifications (PTMs), alternative splicing events and single nucleotide polymorphisms (SNPs) using the technique of Shotgun Annotation developed in the Kelleher Research Group. ProSightPTM is the only proteomics software that allows the user to search their tandem MS data against PTM Warehouses containing the known biological complexity present in UniProt.
Don't guess where the PTMs are, use ProSight.
Generate your free ProSightPTM2 account.
ProSightPC 3.0 allows analysis of Thermo Fisher .RAW LC-MS/MS data. ProSightPC provides:
Contact your local Thermo Fisher sales representative for more information about ProSightPC 3.0, currently launched!!
If your research involves the analysis of neuropeptides, please visit neuroProSight for the unique ability to search for neuropeptides against an annotated prohormone warehouse. neuroProSight is supported by the UIUC Center for Neuroproteomics on Cell-Cell Signaling funded by the National Institute on Drug Abuse Grant P30 DA 018310.
The list of currently supported PTM Warehouses for ProSightPTM is available here.
Dr. John Garavelli is assisting us by incorporating the RESID database of post-translational modifications. We gratefully acknowledge these sources of generous support:
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