Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...
Reexamination Certificate
2007-10-30
2007-10-30
Bragdon, Kathleen Kerr (Department: 1656)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving antigen-antibody binding, specific binding protein...
C435S069100, C435S320100, C435S325000, C530S350000
Reexamination Certificate
active
10388963
ABSTRACT:
The invention provides methods and compositions for protein structure analysis, including substrate binding sites, sites of protein-protein interactions, three dimensional structure analysis, and stability, all with single amino acid resolution. In general, the subject methods involve introduction of cysteine residues, which serve as probes for physical analysis, into a protein by translational misincorporation in vivo. In many embodiments, proteins containing misincorporated cysteine residues are reacted with a crosslinking agent that covalently links misincorporated cysteine residues to a proximal amino acid in the folded protein. These methods, termed “MXLINK” methods, may be used for protein tertiary structure analysis. In other embodiments, cysteine-misincorporated proteins are used in protein footprinting methods, termed “MPAX” or “MSX” methods.
REFERENCES:
patent: WO 00/11208 (2000-03-01), None
patent: WO 00/24922 (2000-05-01), None
Doring Volker et al.Reassigning Cysteine in the Genetic code ofEscherichia coli1998 Genetics 150:543-551.
Karlin et al Sustituted cysteine accessibility Method 1998. Methods in Enzymology 293: 123-145.
Baudouin-Cornu, P., Molecular Evolution of Protein Atomic Composition, Science, 2001, 293: 297-300.
Doring, V., Enlarging the Amino Acid Set ofEscherichia coliby Infiltration of the Valine Coding Pathway, Science, 2001, 292: 501-504.
Doring, V., Reassigning Cysteine in the Genetic Code ofEscherichia coli, Genetics, 1998, 150: 543-551.
Doering, D.S., Cysteine Scanning Mutagensis at 40 of 76 Positions in Villin Headpiece Maps the F-Actin Binding Site and Structural Features of the Domain, Biochemistry, 1996, 35: 12677-12685.
Gygi, S. P. et al., Quantitative Analysis of Complex Protein Mixtures Using Isotope-Coded Affinity Tags, Nature Biotechnology, 1999, 17: 994-999.
Ha, J. et al., Changes in Side Chain Packing During Apomyoglobin Folding Characterized by Pulsed Thioldisulfide Exchange, Nature Structural Biology, 1998, 5(8): 730-737.
Lampert et al., Properties of the Mutant SER-460-CYS Implicate This Site in a Functionally Important Region of the Type IIa Na+/PiCotransporter Protein, J. Gen. Physiol., 1999, 114: 637-651.
Liu, X. et al., Boronate Affinity Chromatography, Methods. Mol. Biol., 2000, 147: 119-28.
Roche, E.D., SSRA-Mediated Peptide Tagging Caused by Rare Condons and TRNA Scarcity, Embo J., 1999, 18(16): 4579-4589.
Sullivan et al., Mapping The Agonist Binding Site of the Nicotinic Acetylcholine Receptor. Orientation Requirements for Activation by Covalent Agonist, J. Biol. Chem., 2000, 275(17): 12651-60.
Tu, B. et al., Protein Footprinting at Cysteines: Probing ATP-Modulated Contacts in Cysteine-Substitution Mutants of Yeast DNA Topoisomerase II, 1999, Proc. Natl. Acad. Sci., 96: 4862-7.
Venkatesan et al., Site-Directed Site-Directed Sulfhydryl Labeling of the Lactose Permease ofEscherichia coli: Helix X., Biochemistry, 2000, 39: 10656-10661.
Venkatesan et al., Site-Directed Site-Directed Sulfhydryl Labeling of the Lactose Permease ofEscherichia coli: N-Ethylmaleimide-Sensitive Face of Helix II, Biochemistry, 2000, 39: 10649-10655.
Venkatesan et al., Site-Directed Sulfhydryl Labeling of the Lactose Permease ofEscherichia coli: Helix VII, 2000, Biochemistry, 39: 10641-10648.
Harbury Pehr A. B.
Martin Warham Lance
Silverman Joshua A.
Bozicevic Field & Francis LLP
Bragdon Kathleen Kerr
Francis Carole L.
Gebreyesus Kagnew
Keddie James S.
LandOfFree
Methods for structural analysis of proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Methods for structural analysis of proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods for structural analysis of proteins will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3833572