Ordered biological nanostructures formed from chaperonin...

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C514S002600, C977S773000

Reexamination Certificate

active

07816491

ABSTRACT:
The following application relates to nanotemplates, nanostructures, nanoarrays and nanodevices formed from wild-type and mutated chaperonin polypeptides, methods of producing such compositions, methods of using such compositions and particular chaperonin polypeptides that can be utilized in producing such compositions.

REFERENCES:
patent: 5428131 (1995-06-01), Trent et al.
patent: 6338952 (2002-01-01), Young
patent: 6858318 (2005-02-01), Kogiso et al.
patent: 2002/0130353 (2002-09-01), Lieber et al.
patent: 2003/0078373 (2003-04-01), Fersht et al.
patent: 2005/0130258 (2005-06-01), Trent et al.
patent: 0 881 691 (1998-02-01), None
patent: 07-067641 (1995-03-01), None
patent: 11-045990 (1999-02-01), None
patent: 11-204774 (1999-07-01), None
patent: WO 00/77196 (2000-12-01), None
patent: WO 03/080796 (2003-10-01), None
Weiss and Goloubinoff Journal of Biological Chemistry 270 (23) : 13956-13960 (1995).
Ursic et al., Molecular Biology of the Cell 5: 1065-1080 (1994), “The essential yeast Tcp1 protein affects actin and microtubules”.
Trent et al., Nature 354(6353): 490-493 (1991), “A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1”.
Shpigel et al., Protein Expression and Purification 14: 185-191 (1998), “Production and purification of a recombinant human hsp60 epitope using the cellulose-binding domain inEscherichia coli”.
Bosch et al., “Crystal structure of the beta-apical domain of the thermosome reveals structural plasticity in the protrusion region”, Journal Molecular Biology 301: 19-25 (Aug. 4, 2000).
Schoehn et al.,“Three conformations of an archael chaperonin, TF55 fromSulfolobus shibatae”, Journal of Molecular Biology 296: 813-819 (Feb. 2000).
Quaite-Randall et al.,“Conformational cycle of the archaesome, a TCP1-like chaperonin fromSulfolobus shibatae”, Journal of Biological Chemistry 270(48): 28818-28823 (1995).
Archibald, et al., Recurrent parology in the evolution of archaeal chaperonins, Current Biology, 1999, 1053-1056, 9-18, Elsevier Science Ltd.
Bayburt, et al., Structure, Behavior, and Manipulation of Nanoscale Biologica . . . , Handbook of Nanostructured Materials and Nanotechnology, 2000, 637-710, 5, Academic Press.
Beernink, et al., Random circular permutation leading to chain disruption within and . . . , Protein Science, 2001, 528-537, 10, Cold Spring Harbor Lab. Press.
Berven, et al., Defect-Tolerant Single-Electron Charging at Room Temperature in Metal Nanoparticle Decorated B . . . , Adv. Mater., 2001, 109-113, 13-2, WILEY-VCH-Verlag GmbH.
Brown, et al., a Genetic Analysis of Crystal Growth, J. Mol. Biol. 2000, 725-735, 299, Academic Press.
Brown, Metal-recognition by repeating polypeptides, Nature Biotechnol. 1997, 269-272, 15.
Bruchez, et al., Semiconductor Nanocrystals as Fluorescent Biological Labels, Science, 1998, 2013-2016, 281, AAAS.
Chan, et al., Quantum Dot Bioconjugates for Ultrasensitive Nonisotopic Detection, Science, 1998, 2016-2018, 281, AAAS.
Charlebois, et al.,Sulfolobusgenome: from genomics to biology, Curr. Opin. in Microbio., 1998, 584-588, 1.
Dabbousi, et al., (CdSe)ZnS Core-Shell Quantum Dots: Synthesis and Characterization of a Size Series . . . , J. Phys. Chem. B, 1997, 9463-9475, 101, American Chemical Society.
Dat, et al., Mimicking a conformational B cell epitope of the heat shock protein PfHsp70-1 antigen of Pla . . . , Parasite Immunology, 2000. 535-543, 22, Blackwell Science Ltd.
Ditzel, et al., Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCT, Cell Press, 1998, 125-138, 93, Cell Press.
Douglas, et al., Nanometer molecular lithography, 1986, Appl. Phys. Lett., 676-678, 48.
Douglas, et al., Virus Particles as Templates for Materials Synthesis, Adv. Mater., 1999, 679-681, 11-8, Wiley-VCH-Verlag GmbH.
Douglas, et al., Host-guest encapsulation of materials by assembled virus protein cages, Nature, 1998, 152-155, 393, Macmillan Publishers Ltd.
Dujardin, et al., Bio-inspired Materials Chemistry, Adv. Mater, 2002, 775-788, 14-11, WILEY-VCH Verlag GMbH.
Ellis, et al., Two-Dimensional Crystallization of the Chaperonin TF55 from the Hyperthermophilic Archaeon Sulfolobus . . . , J. Struc. Biol., 1998, 30-36, 123, Academic Press.
Fenton, et al., GroEL-mediated protein folding, Protein Science, 1997, 743-760, 6, Cold Spring Harbor Laboratory Press.
Furutani, et al., Group II Chaperonin in a Thermophilic Methanoge . . . , J. Biol. Chem., 1998, 28399-28407, 273-43, American Society for Biochemistry & Molecular Biology, Inc.
Galagan, et al., The Genome of M. acetivorans Reveals Extensive Metabolic and Physiological Diversity, Genome Research, 2002, 532-542, 12, Cold Spring Harbor Laboratory Press.
Gerion, et al., Synthesis and Properties of Biocompatible Water-Soluble Silica-Coated CdSe/ZnS Semico . . . , J. Phys. Chem. B, 2001, 8861-8871, 105, American Chemical Society.
Gerstein, et al, Comprehensive assessment of automatic structural alignment against a manual sta . . . , Protein Science, 1998, 445-456, 7, Cold Spring Harbor Laboratory Press.
Gerstein, et al., Using Iterative Dynamic Programming to Obtain Accurate Pairwise and Multiple Al . . . , Proc. of ISMB-96, 1996, 59-67, 96, AAAI Press, Menlo Park, California.
Griesbeck, et al., Reducing the Environmental Sensitivity of Yel . . . , J. Biol. Chem., 2001, 29188-29194, 276-31, American Society for Biochemistry & Molecular Biology, Inc.
Guex, et al., Protein modelling for all, TiBS, 1999, 364, 24.
Guex, et al., SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling, Electrophoresis, 1997, 2714-2723, 18-15.
Hall, et al., Site-Specific Organization of Gold Nanoparticles by Biomolecular Templating CHEMPHYSCHEM, 2001, 184-186,3, WILEY-VCH-Verlag GmbH.
Harris, et al., Electron Microscopy of the GroEL-GroES Filament, J. Structural Biol., 1995, 68-77, 115, Academic Press, Inc.
Hartl, Molecular chaperones in cellular protein folding, Nature, 1996, 571-580, 381.
Hartl, et al., Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein, Science, 2002, 1852-1858, 295.
Heinemann, et al., Circular Permutation of Polypeptide Chains: Implications for Protein Folding and Stability, Prog. Biophys. Mol. Biol., 1995, 121-143, 64.
Horwich, et al., Protein folding in the cell: functions of two families of molecular chaperone, hsp60 and TF55-TCP1, Phil. Trans R. Soc. Lond., 1993, 313-326, 339.
Hulteen, et al., Nanosphere lithography: A materials general fabrication process for periodic p . . . , J. Vac. Sci. Technol. A, 1995, 1553-1558, 13-3, American Vacuum Society.
Iwakura, et al., Systemic circular permutation of an entire protein reveals essential folding elements, Nat. Struct. Biol., 2000, 580-585, 7.
Kagawa, et al., The 60 kDa Heat Schock Proteins in the Hyperthermophilic ArchaeonSulfolobus shibatae, J. Mol. Biol., 1995, 712-725, 253, Academic Press Ltd.
Kagawa, et al., The composition, structure and stability of a group II chaperonin are temperature regulated in a hyperthermophilic . . . , Molec Microbio, 2003, 143-156, 48-1.
Karlin, et al., Characterizations of Highly Expressed Genes of Four Fast-Growing Bacteria, J. Bacteriol., 2001, 5025-5040, 183-17, American Society for Microbiology.
Keren, et al., Sequence-Specific Molecular Lithography on Single DNA Molecules, Science, 2002, 72-75, 297.
Klumpp, et al., The thermosome: archetype of group II chaperonins, FEBS Letters, 1998, 73-77, 430, Federation of European Biochemical Societies.
Koeck, et al., Two-dimensional crystals of reconstituted B-subunits of the chaperonin TF55 fromSulfolobus shibatae, Biochim. Biophys. Acta, 1998, 40-44, 1429-1.
Kramer, et al., Engineered protein cages for nanomaterial synthesis, J. Am. Chem. Soc., 2004, 13282-13286, 126-41.
Kroger, et al., Polycationic Peptides from Diatom Biosilica That Direct Silica Nanosphere Formation, Science, 1999, 1129-1132, 286.
Labas, et al., Diversity and evolution of the green fluorescent protein family, Proc Natl Acad Sci USA, 2002, 4256-4261, 99.
Lee, et a

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Ordered biological nanostructures formed from chaperonin... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Ordered biological nanostructures formed from chaperonin..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Ordered biological nanostructures formed from chaperonin... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-4213490

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.