Chemistry: electrical and wave energy – Processes and products – Electrophoresis or electro-osmosis processes and electrolyte...
Reexamination Certificate
2008-07-01
2008-07-01
Weber, Jon P (Department: 1657)
Chemistry: electrical and wave energy
Processes and products
Electrophoresis or electro-osmosis processes and electrolyte...
C436S002000
Reexamination Certificate
active
07393443
ABSTRACT:
The present invention provides a fast and efficient means for identifying kinetically stable proteins. As used herein the term “kinetically stable protein” means a protein that is trapped in a specific conformation due to an unusually high unfolding barrier that results in very slow unfolding rates. The present inventors are the first to discover the existence of a correlation between kinetic stability and SDS-induced denaturation. Thus, the invention provides methods for identifying kinetically stable proteins comprising the step of testing the proteins for resistance to denaturation by SDS. In one embodiment, SDS-polyacrylamide gel electrophoresis (SDS-PAGE) is one simple method for quickly identifying and selecting kinetically stable proteins.
REFERENCES:
patent: 5360729 (1994-11-01), Bartfeld et al.
patent: 5681711 (1997-10-01), Bredesen
patent: 5710033 (1998-01-01), Hallewell et al.
patent: 5843641 (1998-12-01), Brown et al.
patent: 6331421 (2001-12-01), Hallewell et al.
patent: 2002/0164635 (2002-11-01), Salerno
patent: 2004/0219570 (2004-11-01), Salerno
Fasshauer et al. Structural Changes are Associated With Soluble N-Ethylmaleimide-Sensitive Fusion Protein Attachment Protein Receptor Complex Formation; The Journal of Biological Chemistry, vol. 272, No. 44 (1997) pp. 28036-28041.
Stoll et al. Protein Microarray Technology; Frontiers in Bioscience, vol. 7, c13-32 (2002).
Jin et al. Dynamic Labeling During Capillary or Microchip Electrophoresis for Laser-Induced Fluorescence Detection of Protein-SDS Complexes Without Pre or Postcolumn Labeling; Analytical Chemistry, vol. 73, No. 20 (2001) pp. 4994-4999.
Fasshauer et al. Snare Assembly and Disassembly Exhibit a Promouned Hysteresis; Nature Structural Biology, vol. 9. No. 2 (2002) pp. 144-151.
Jin et al. Dynamic Labeling During Capillary or Microchip Electrophoresis for Laser-Induced Fluorescence Detection of Protein-SDS Complexes Without Pre or Postcolumn Labeling; Analytical Biochemistry, vol. 73, No. 20 (2001) pp. 4994-4999.
Shusta et al. Yeast Surface Display for Directed Evolution of Protein Expression, Affinity, and Stability; Methods in Enzymology, vol. 328 (2000) pp. 430-444.
Nelson, C. The Binding of Detergents to Proteins; The Journal of Biological Chemistry, vol. 246, No. 12 (1971) pp. 3895-3901.
Radunović, A. et al., “Cu/Zn Superoxide Dismutase Gene Mutations in Amyotrophic Lateral Sclerosis: Correlation Between Genotype and Clinical Features,”J. Neurology, Neurosurgery, and Psychiatry, 61: 565-572 (1996).
Juneja, T. et al., “Prognosis in Familial Amyotrophic Lateral Sclerosis: Progression and Survival in Patients with Glu100gly and Ala4val Mutations in Cu, Zn, Superoxide Dismutase,”Neurology, 48(1): 55-57 (1997).
Cudkowicz, M.E., et al., “Epidemiology of Mutations in Superoxide Dismutase in Amyotrophic Lateral Sclerosis,”Ann. Neuro., 41: 210-221 (1997).
Subramaniam, Jamuna R., et al., “Mutant SOD1 Causes Motor Neuron Disease Independent of Copper Chaperone-Mediated Copper Loading,”Nat. Neurosci., 5(4): 301-307 (2002).
Beckman, J.S., et al., “CCS Knockout Mice Establish an Alternative Source of Copper for SOD in ALS,”Free Radic. Biol.&Med., 33(10): 1433-1435 (2002).
Bush, A.I., “Is ALS Caused by an Altered Oxidative Activity of Mutant Superoxide Dismutase,”Nat. Neurosci., 5(10): 919-920 (2002).
“Drug Development and Clinical Trials: Drug Development Updates,” retrieved from the Internet on Apr. 18, 2003. <http://alsa.org/research/drugdev.cfm>.
Morrison, Karen E., “Therapies in Amyotrophic Lateral Sclerosis-Beyond Riluzole,”Current Opinion in Pharmacology, 2: 302-309 (2002).
Hardy, John and Gwinn-Hardy, Katrina, “Neurodegenerative Disease: A Different View of Diagnosis,”Molecular Medicine Today, 5: 514-517 (1999).
Mathisen, Peter M., “Gene Discovery and Validation for Neurodegenerative Diseases,”DDT, 8(1): 39-46 (2003).
Wang, Limin, et al., “Murine Apolipoprotein Serum Amyloid A in Solution Forms a Hexamer Containing a Central Channel,”PNAS, 99(25): 15947-15952 (2002).
Cunningham, E.L., et al., “Kinetic Stability as a Mechanism for Protease Longevity,”Proc. Natl. Acad. Sci. USA, 96: 11008-11014 (1999).
Ohnishi, S. And Kameyama, K., “Escherichia coliOmpA Retains a Folded Structure in the Presence of Sodium Dodecyl Sulfate Due to a High Kinetic Barrier to Unfolding,”Biochim. Biophys. Acta, 1515: 159-166 (2001).
Kaushik, J.K., et al., The Unusually Slow Relaxation Kinetics of the Folding-Unfolding of Pyrrolidone Carboxyl Peptidase from a Hyperthermophile, Pyrococcus Furiosus,J. Mol. Biol., 316: 991-1003 (2002).
Colón Wilfredo
Manning Marta
Elmore Carolyn S.
Elmore Patent Law Group P.C.
Martin Paul C.
Rensselaer Polytechnic Institute
Vanstone Darlene A.
LandOfFree
Methods of identifying kinetically stable 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 of identifying kinetically stable proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods of identifying kinetically stable proteins will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2752830