Phase sensitively-detected reduced dimensionality nuclear...

Chemistry: analytical and immunological testing – Nuclear magnetic resonance – electron spin resonance or other...

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

Reexamination Certificate

active

07396685

ABSTRACT:
The present invention discloses eleven reduced dimensionality (RD) triple resonance nuclear magnetic resonance (NMR) experiments for measuring chemical shift values of certain nuclei in a protein molecule, where the chemical shift values encoded in a peak pair of an NMR spectrum are detected in a phase sensitive manner. The RD 3DHA,CA,(CO),N,HN NMR and RD 3DH,C,(C-TOCSY-CO),N,HN NMR experiments are designed to yield “sequential” connectivities, while the RD 3DHα/β,Cα/β,CO,HA NMR and RD 3DHα/β,Cα/β,N,HN NMR experiments provide “intraresidue” connectivities. The RD 3DH,C,C,H-COSY NMR, RD 3DH,C,C,H-TOCSY NMR, and RD 2DH,C,H-COSY NMR experiments allow one to obtain assignments for aliphatic and aromatic side chain chemical shifts, while the RD 2DHB,CB,(CG,CD),HD NMR experiment provide information for the aromatic side chain chemical shifts. In addition, methods of conducting suites of RD triple resonance NMR experiments for high-throughput resonance assignment of proteins and determination of secondary structure elements are disclosed.

REFERENCES:
Fernández et al., “NMR with13C,15N-Doubly-Labeled DNA: TheAntennapediaHomeodomain Complex with a 14-mer DNA Duplex,”Journal of Biomolecular NMR12:25-37 (1998).
Gehring et al., “H(C)CH-COSY and (H)CCH-COSY Experiments for13C-Labeled Proteins in H2O Solution,”Journal of Magnetic Resonance135:185-193 (1998).
Yamazaki et al., “Two-Dimensional NMR Experiments for Correlating13Cβ and1Hδ/ε Chemical Shifts of Aromatic Residues in13C-Labeled Proteins via Scalar Couplings,”J. Am. Chem. Soc. 115:11054-11055 (1993).
Shirra, “Three Dimensional NMR Spectroscopy,” http://www.cryst.bbk.ac.uk/PPS2/projects/schirra/html/3dnmr.htm (1996).
Pang et al., “High-Resolution Detection of Five Frequencies in a Single 3D Spectrum: HNHCACO—A Bidirectional Coherence Transfer Experiment,”Journal of Biomolecular NMR11:185-1990 (1998).
Gardner et al., “The Use of2H,13C,15N Multidimensional NMR to Study the Structure and Dynamics of Proteins,”Annu. Rev. Biophys. Biomol. Struct. 27:357-406 (1998).
Sattler et al., “Triple Resonance Pulse Programs for13C,15N Labeled Proteins,” http://www/embl-heidelberg.de
mr/sattler/PP/pulseprograms.html (2001).
Tugarinov et al., “Four-Dimensional NMR Spectroscopy of a 723-Residue Protein: Chemical Shift Assignments and Secondary Structure of Malate Synthase G,”J. Am. Chem. Soc. 124:10025-10035 (2002).
Kennedy et al., “Role for NMR in Structural Genomics,”Journal of Structural and Functional Genomics2:155-169 (2002).
Szyperski et al., “Reduced Dimensionality in Triple-Resonance NMR Experiments,”J. Am. Chem. Soc., 115:9307-9308 (1993).
Szyperski et al., “3D13C-15N-Heteronuclear Two-Spin Coherence Spectroscopy for Polypeptide Backbone Assignments in13C-15N-Double-Labeled Proteins,”J. Biomol. NMR, 3:127-132 (1993).
Szyperski et al., “3D Hα/βCα/β(CO)NHN, a Projected 4D NMR Experiment for Sequential Correlation of Polypeptide1Hα/β,13Cα/βand Backbone15N and1HNChemical Shifts,”J. Magn. Reson., B105:188-191 (1994).
Szyperski et al., “A Novel Reduced-Dimensionality Triple-Resonance Experiment for Efficient Polypeptide Backbone Assignment, 3D CO HN N CA,”J. Magn. Reson., B108:197-203 (1995).
Szyperski et al., “Useful Information from Axial Peak Magnetization in Projected NMR Experiments,”J. Am. Chem. Soc., 118:8146-8147 (1996).
Szyperski et al., “Two-Dimensionalct-HC(C)H-COSY for Resonance Assignments of Smaller13C-Labeled Biomolecules,”J. Magn. Reson., 128:228-232 (1997).
Szyperski et al., “Sequential Resonance Assignment of Medium-Sized15N/13C-Labeled Proteins with Projected 4D Triple Resonance NMR Experiments,”J. Biomol. NMR, 11:387-405 (1998).
Liu et al., “NMR Experiments for Resonance Assignments of13C,15N Doubly-Labeled Flexible Polypeptides: Application to Human Prion Protein hPrP(23-230),”J. Biomol. NMR, 16:127-138 (2000).
Yamazaki et al., “Assignments of Backbone1H,13C, and15N Resonances and Secondary Structure of Ribonuclease H fromEscherichia coliby Heteronuclear Three-Dimensional NMR Spectroscopy,”Biochemistry, 30:6036-6047 (1991).
Brutscher et al., “Determination of an Initial Set of NOE-Derived Distance Constraints for the Structure Determination of15N/13C-Labeled Proteins,”J. Magn. Reson., B109:238-242 (1995).
Szyperski et al., “Reduced-Dimensionality NMR Spectroscopy For High-Throughput Protein Resonance Assignment,”PNAS, 99:8009-8014 (2002).

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

Phase sensitively-detected reduced dimensionality nuclear... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Phase sensitively-detected reduced dimensionality nuclear..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Phase sensitively-detected reduced dimensionality nuclear... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2758131

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