Monitoring Protein-Drug Interactions with Mass Spectrometry and Proteolysis Protein Mass Mapping as a Drug Assay
نویسندگان
چکیده
منابع مشابه
Mapping protein-protein interactions by affinity-directed mass spectrometry.
A precise and rapid method for identifying sites of interaction between proteins was demonstrated; the basis of the method is direct mass spectrometric readout from the complex to determine the specific components of the proteins that interact--a method termed affinity-directed mass spectrometry. The strategy was used to define the region of interaction of a protein growth factor with a monoclo...
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iii ACKNOWLEDGEMENTS I would like to acknowledge and thank the people who have supported me throughout my higher educational career. I had the privilege of working along side Son Nguyen in the lab as he welcomed me aboard this project. Son showed me the ropes as we progressed through this tedious and exciting research. I want to thank him specifically for his patience when experiments went astr...
متن کاملProtein epitope mapping by mass spectrometry.
A mass spectrometric method is described for the rapid mapping of linear epitopes in proteins that are bound by monoclonal antibodies. The method consists of three steps. In the first step, an antigen protein is digested by a proteolytic enzyme to produce an appropriate set of peptide fragments. In the second step, peptide fragments containing the linear epitope are selected and separated from ...
متن کاملMass spectrometry for the study of protein-protein interactions.
The identification of subpicomolar amounts of protein by mass spectrometry (MS) coupled with two-dimensional methods to separate complex protein mixtures is fueling the field of proteomics, and making feasible the notion of cataloging and comparing all of the expressed proteins in a biological sample. Functional proteomics is a complementary effort aimed at the characterization of functional fe...
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ژورنال
عنوان ژورنال: JALA: Journal of the Association for Laboratory Automation
سال: 1999
ISSN: 1535-5535
DOI: 10.1016/s1535-5535-04-80012-1