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.
A article describing the new features in ProSight PTM 2.0 can be found on-line:
ProSight PTM 2.0: improved protein identification and characterization for top down mass spectrometry
Leonid Zamdborg; Richard D. LeDuc; Kevin J. Glowacz; Yong-Bin Kim; Vinayak Viswanathan; Ian T. Spaulding; Bryan P. Early; Eric J. Bluhm; Shannee Babai; Neil L. Kelleher
Nucleic Acids Research 2007; doi: 10.1093/nar/gkm371
A tool for determining all protein forms in a ProSight proteome warehouse that have a theoretical mass within a user-specified tolerance of a given value
Rattus norvegicus, Mus musculus, Homo sapiens
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ProSight PTM 2.0 allows identification and characterization of intact proteins and their post- translational modifications (PTMs) using the Top-Down Approach. This site has many tools and graphical features to facilitate analysis of single (recombinant) proteins, proteins in mixtures, and proteins fragmented in parallel.
If you are interested in obtaining a free account for academic research, please send an email to prosightptm@scs.uiuc.edu.
The list of currently supported databases 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:
ProSight PTM 2.0 was developed by The Kelleher Group
of the Department of Chemistry at the University of Illinois at Urbana-Champaign.
© Copyright 2005 The Board of Trustees of the University of Illinois.