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Identification of phosphotyrosine (pTyr)-containing T cell proteins

ABSTRACT: This project aimed at identifying phosphotyrosine (pTyr)-containing T cell proteins that bind directly to the pTyr-binding pocket in the N-terminal C2 domain of protein kinase C-theta. We used an immobilized recombinant GST-C2 fusion protein to pull-down proteins present in lysates of stimulated human leukemic Jurkat T cell line. After eluting and separating C2-bound proteins by SDS-PAGE, protein bands in the ~60-70 kDa range detected by Coomassie blue staining or anti-pTr immunoblotting were excised from the gel, destained, and subjected to trypsinization. The resulting peptides were extracted, dried, dissolved in 0.1% formic acid, and analyzed by online nano flow LC-MS/MS.

INSTRUMENT(S): LTQ Orbitrap, 1200 series LC/MSD SL

ORGANISM(S): Homo sapiens

SUBMITTER: Amnon Altman

PROVIDER: MSV000083562 | Massive | Wed Mar 13 11:19:00 GMT 2019

REPOSITORIES: MassIVE

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Project description:Auer2010 - Correlation between lag time and aggregation rate in protein aggregation This model is described in the article: Insight into the correlation between lag time and aggregation rate in the kinetics of protein aggregation. Auer S, Kashchiev D. Proteins 2010 Aug; 78(11): 2412-2416 Abstract: Under favorable conditions, many proteins can assemble into macroscopically large aggregates such as the amyloid fibrils that are associated with Alzheimer's, Parkinson's, and other neurological and systemic diseases. The overall process of protein aggregation is characterized by initial lag time during which no detectable aggregation occurs in the solution and by maximal aggregation rate at which the dissolved protein converts into aggregates. In this study, the correlation between the lag time and the maximal rate of protein aggregation is analyzed. It is found that the product of these two quantities depends on a single numerical parameter, the kinetic index of the curve quantifying the time evolution of the fraction of protein aggregated. As this index depends relatively little on the conditions and/or system studied, our finding provides insight into why for many experiments the values of the product of the lag time and the maximal aggregation rate are often equal or quite close to each other. It is shown how the kinetic index is related to a basic kinetic parameter of a recently proposed theory of protein aggregation. This model is hosted on BioModels Database and identified by: BIOMD0000000555. To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.