Brian T. Chait - N.Y. NY David Cowburn - Westfield NJ Yoshi Oda - Ibaraki, JP
Assignee:
The Rockefeller University - New York NY
International Classification:
G01N 3100
US Classification:
436173, 436174, 436177
Abstract:
The present invention is a method for accurately comparing the levels of cellular components, such as proteins, present in samples which differ in some respect from each other using mass spectroscopy and isotopic labeling. A first sample of biological matter, such as cells, is cultured in a first medium and a second sample of the same biological matter is cultured in a second medium, wherein at least one isotope in the second medium has a different abundance than the abundance of the same isotope in the first medium. One of the samples is modulated, such as by treatment with a bacteria, a virus, a drug, hormone, a chemical or an environmental stimulus. The samples are combined and at least one protein is removed. The removed protein is subjected to mass spectroscopy to develop a mass spectrum. A ratio is computed between the peak intensities of at least one closely spaced pair of peaks to determine the relative abundance of the protein in each sample.
Method For The Comparative Quantitative Analysis Of Proteins And Other Biological Material By Isotopic Labeling And Mass Spectroscopy
Brian T. Chait - N.Y. NY David Cowburn - Westfield NJ Yoshi Oda - Ibaraki, JP
Assignee:
The Rockefeller University - New York NY
International Classification:
G01N 2400
US Classification:
436173, 436174, 436177
Abstract:
The present invention is a method for accurately comparing the levels of cellular components, such as proteins, present in samples which differ in some respect from each other using mass spectroscopy and isotopic labeling. A first sample of biological matter, such as cells, is cultured in a first medium and a second sample of the same biological matter is cultured in a second medium, wherein at least one isotope in the second medium has a different abundance than the abundance of the same isotope in the first medium. One of the samples is modulated, such as by treatment with a bacteria, a virus, a drug, hormone, a chemical or an environmental stimulus. The samples are combined and at least one protein is removed. The removed protein is subjected to mass spectroscopy to develop a mass spectrum. A ratio is computed between the peak intensities of at least one closely spaced pair of peaks to determine the relative abundance of the protein in each sample.
Methods And Devices For Characterizing Macromolecular Complexes Using Isotope Labeling Techniques
David Cowburn - Westfield NJ, US Kaushik Dutta - New York NY, US Fabien Ferrage - New York NY, US Alexander Shekhtman - Albany NY, US
International Classification:
G01N 33/53 G06F 19/00
US Classification:
435007100, 702019000
Abstract:
A method for characterizing interactions in macromolecular complexes, such as protein-protein or protein-ligand complexes, by selective isotopic labeling of the target molecule to reduce the H density in a selected spectral region; by irradiating the target; and by monitoring the polarization using filtered nuclear Overhauser spectroscopy (NOESY) and/or by performing selective saturation transfer experiments to determine the docking potential of the macromolecular complex.
Beatrice S. Knudsen - New York NY Stephan M. Feller - New York NY John Kuriyan - New York NY Xiaodong Wu - New York NY Jie Zheng - New York NY David Cowburn - Westfield NJ
Assignee:
The Rockefeller University - New York NY
International Classification:
C12P 2106 C12N 120 C07H 2100
US Classification:
435 691
Abstract:
The present invention relates to regulation and control of cellular processes by SH3-domain binding proteins and peptides. In particular, the invention provides a consensus sequence of a peptide that shows high specificity and affinity for the first SH3 domain of cellular Crk. In specific examples, a number of peptides that contain the consensus are shown to bind c-Crk specifically. The molecular basis for this specificity is examined by crystallography.
Method Of Determining Interdomain Orientation And Changes Of Interdomain Orientation On Ligation
David Cowburn - Westfield NJ Rong Xu - Tarrytown NY David Fushman - New York NY
Assignee:
The Rockefeller University - New York NY
International Classification:
G01N 3353 G01N 33566 G01N 33557
US Classification:
435 71
Abstract:
The present invention provides methods for determining the relative orientation of the individual components of a macromolecule in solution with respect to the global molecular coordinate frame of the macromolecule. The present invention further provides methods for applying this structural information, including for rational drug design.
- Princeton NJ, US - Bronx NY, US JOSEF GRAMESPACHER - Princeton NJ, US DAVID COWBURN - Bronx NY, US GIRIDHAR SEKAR - Bronx NY, US
International Classification:
C07K 14/00 C07K 1/02
Abstract:
The present disclosure relates to atypical split N- and C-inteins and variants thereof. This disclosure also relates to complexes comprising the split N- or C-inteins of this disclosure and a compound of interest and compositions comprising said complexes. In addition, this disclosure relates to methods of using the atypical split N- and C-inteins.
New York Structural Biology Center
Member Board of Directors
Coferon Jun 2009 - Nov 2010
Sab Member
Albert Einstein College of Medicine Jun 2009 - Nov 2010
Professor
New York Structural Biology Center Sep 2000 - Aug 2010
President and Ceo; Head, Lab Physical Biochemistry
Rockefeller University 1972 - 2001
Faculty
Education:
King's College London 1981 - 1981
Columbia University Vagelos College of Physicians and Surgeons 1970 - 1973
King's College London 1965 - 1970
Doctorates, Doctor of Philosophy, Biophysics
The University of Manchester 1962 - 1965
Manchester Grammar School 1956 - 1962
Skills:
Structural Biology Biophysics Biochemistry Molecular Biology Nmr Protein Chemistry Science Bioinformatics Life Sciences Cell Biology Signal Transduction Protein Purification Drug Discovery Protein Expression Lifesciences Chemistry Spectroscopy Homology Modeling Fluorescence X Ray Crystallography Computational Biology Cancer Pharmacology Molecular Cloning Molecular Modeling Pcr Purification Nuclear Magnetic Resonance
Interests:
Civil Rights and Social Action Education Science and Technology Human Rights Health