Selected Ubiquitin Bibliography
Introduction Function Sequence Details BMRB and PDB entries Bibliography

NMR Publications

  • Early Papers
    1. Goldstein, G., Scheid, M., Hammerling, U., Boyse, E. A., Schlesinger, D. H., Niall, H. D. (1975) Isolation of a Polypeptide that has Lymphocite-Differentiating Properties and is probably represented universally in living cells. Proc. Natl. Acad. Sci. USA 72, pp. 11-15.
    2. Schlesinger, D. H., Goldstein, G., Niall, H. D. (1975) Complete Amino Acid Sequence of Ubiquitin, an Adenylate Cyclase stimulating polypeptide probably universal in living cells. Biochemistry (N. Y.) 14, 2214-2218.
    3. Hershko, A., Ciechanover, A., and Rose, I.A. (1979) Resolution of the ATP-dependent proteolytic system from reticulocytes: A component that interacts with ATP. Proc. Natl. Acad. Sci. USA 76, pp. 3107-3110.
    4. Hershko, A., Ciechanover, A., Heller, H., Haas, A.L., and Rose I.A. (1980) Proposed role of ATP in protein breakdown: Conjugation of proteins with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc. Natl. Acad. Sci. USA 77, pp. 1783-1786.
    5. Hershko, A., Ciechanover, A., Heller, H., Haas, A.L., and Rose I.A. (1980) Proposed role of ATP in protein breakdown: Conjugation of proteins with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc. Natl. Acad. Sci. USA 77, pp. 1783-1786.

  • 2004
    1. Bouguet-Bonnet, S., Mutzenhardt, P., Canet, D. (Oct 2004) Measurement of 15N csa/dipolar cross-correlation rates by means of Spin State Selective experiments. J. Biomol. NMR 30, 2, 133-142.
    2. Xia Y., Zhu G., Veeraraghavan, S., Gao, X. (Aug 2004) (3,2)D GFT-NMR experiments for fast data collection from proteins. J. Biomol. NMR 29, 4, 467-476.
    3. Lincong Wang, L. Donald, B. R. (Jul 2004) Exact Solutions for Internuclear Vectors and Backbone Dihedral Angles from NH Residual Dipolar Couplings in Two Media, and their Application in a Systematic Search Algorithm for Determining Protein Backbone Structure. J. Biomol. NMR 29, 3, 223-242.
    4. Lancelot, N., Elbayed, K., Bianco, A. (Jul 2004) Measurement of Scaled Residual Dipolar Couplings in Proteins Using Variable-angle Sample Spinning. J. Biomol. NMR, 29, 3, 259-269.
    5. Jaravine, V. A., Cordier, F., Grzesiek, S. (Jul 2004) Quantification of H/D Isotope Effects on Protein Hydrogen-bonds by h3JNC' and 1JNC' Couplings and Peptide Group 15N and 13C' Chemical Shifts. J. Biomol. NMR, 29, 3, 309-318.
    6. Langmead, C. J., Donald, B. R. (Jun 2004) An expectation/maximization nuclear vector replacement algorithm for automated NMR resonance assignments. J. Biomol. NMR 29, 2, 111-138.
    7. Bougault, C., Feng, L., Glushka, J., Kupce, E., Prestegard, J. H. (Apr 2004) Quantitation of rapid proton-deuteron amide exchange using hadamard spectroscopy. J. Biomol. NMR 28, 4, 385-390.
    8. Kupce, E., Freeman, R. (Apr 2004) Fast reconstruction of four-dimensional NMR spectra from plane projections. J. Biomol. NMR 28, 4, 391-395.
    9. Majumdar, A., Ghose, R. (Mar 2004) Probing Slow Backbone Dynamics in Proteins Using TROSY-Based Experiments to Detect Cross-Correlated Time-Modulation of Isotropic Chemical Shifts. J. Biomol. NMR 28, 3, 213-227.
    10. Wist, J., Frueh, D., Tolman, J. R., Bodenhausen, G. (Mar 2004) Triple Quantum Decoherence under Multiple Refocusing: Slow Correlated Chemical Shift Modulations of C' and N Nuclei in Proteins. J. Biomol. NMR 28, 3, 263-272.
    11. Vugmeyster, L., Perazzolo, C., Wist, J., Frueh, D., Bodenhausen, G. (Feb 2004) Evidence of Slow Motions by Cross-Correlated Chemical Shift Modulation in Deuterated and Protonated Proteins. J. Biomol. NMR 28, 2, 137-177.
    12. Tuttle, T., Kraka, E., Wu, A. and Cremer, D. (2004) Investigation of the NMR Spin--Spin Coupling Constants across the Hydrogen Bonds in Ubiquitin: The Nature of the Hydrogen Bond as Reflected by the Coupling Mechanism as Reflected by the Coupling Mechanism. J. Am. Chem. Soc. 126, 16 5093-5107.
    13. Tenno, T., Fujiwara, K., Tochio, H., Iwai, K., Morita, E. H., Hayashi, H., Murata, S., Hiroaki, H., Sato, M., Tanaka, K. and Shirakawa, M. (2004) Structural basis for distinct roles of Lys63- and Lys48-linked polyubiquitin chains. Genes to Cells 9, 865-875.
    14. Scott, P. M., Bilodeau, P. S., Zhdankina, O., Winistorfer, S. C., Hauglund, M. J., Allaman, M. M., Kearney, W. R., Robertson, A. D., Boman, A. L. and Piper, R. C. (2004) GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network. Nat. Cell Biol. 6, 8-2.
    15. Massi, F., Johnson, E., Wang, C., Rance, M. and Palmer, A. G. (2004) NMR R1n Rotating-Frame Relaxation with Weak Radio Frequency Fields. J. Am. Chem. Soc. 126, 2247-2256.
    16. Clore, G. M., Schwieters, C. D. (2004) How Much Backbone Motion in Ubiquitin Is Required To Account for Dipolar Coupling Data Measured in Multiple Alignment Media as Assessed by Independent Cross-Validation? J. Am. Chem. Soc. 126, 9, 2923-2938.
    17. Igumenova, T. I., Wand, A. J. and McDermott, A. E. (2004) Assignment of the Backbone Resonances for Microcrystalline Ubiquitin. J. Am. Chem. Soc. 126, 5323-5331.
    18. Igumenova, T. I., McDermott, A. E., Zilm, K. W., Martin, R. W., Paulson, E. K. and Wand, A. J. (2004) Assignments of Carbon NMR Resonances for Microcrystalline Ubiquitin. J. Am. Chem. Soc. 126, 6720-6727.
    19. Cordier, F., Grzesiek, S. (2004) Quantitative Comparison of the Hydrogen Bond Network of A-State and Native Ubiquitin by Hydrogen Bond Scalar Couplings. Biochemistry 43, 35, 11295-11301.
    20. Benitez-Cardoza, C. G., Stott, K., Hirshberg, M., Went, H. M., Woolfson, D. N., Jackson, S. E. (2004) Exploring Sequence/Folding Space: Folding Studies on Multiple Hydrophobic Core Mutants of Ubiquitin. Biochemistry 43, 18, 5195-5203.

  • 2003
    1. Permi, P. (Dec 2003) Measurement of residual dipolar couplings from 1HA to 13CA and 15N using a simple HNCA-based experiment. J. Biomol. NMR 27, 4, 341-349.
    2. Kupce, E., Freeman, Rl (Dec 2003) Reconstruction of the three-dimensional NMR spectrum of a protein from a set of plane projections. J. Biomol. NMR 27, 4, 383-387.
    3. Gehman, J. D., Paulson, E. K. Zilm, K. W. (Nov 2003) The influence of internuclear spatial distribution and instrument noise on the precision of distances determined by solid state NMR of isotopically enriched proteins. J. Biomol. NMR 27, 3, 383-387.
    4. Carlomagno, T., Bermel, W., Griesinger, C. (Oct 2003) Measuring the X1 torsion angle in protein by CH-CH cross-correlated relaxation: A new resolution-optimised experiment. J. Biomol. NMR 27, 2, 383-387.
    5. Jin, C., Prompers, J. J., Bruschweiler, R. (Jul 2003) Cross-correlation suppressed T1 and NOE experiments for protein side-chain 13CH2 groups. J. Biomol. NMR 26, 3, 241-247.
    6. Kozminski, W., Zhukov, I. (Jun 2003) Multiple quadrature detection in reduced dimensionality experiments. J. Biomol. NMR 26, 2, 157-166.
    7. Pelupessy, P., Ravindranathan, S., Bodenhausen, G. (Apr 2003) Correlated motions of successive amide N-H bonds in proteins. J. Biomol. NMR 25, 4, 265-280.
    8. Babu C.R., Flynn, P. F., Wand, A. J. (Apr 2003) Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids. J. Biomol. NMR 25, 4, 313-323.
    9. Ishima, R., Torchia, D. A. (Mar 2003) Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach. J. Biomol. NMR 25, 3, 243-248.
    10. Giesen, A. W., Homans, S. W. Brown, J. M. (Jan 2003) Determination of protein global folds using backbone residual dipolar coupling and long-range NOE restraints. J. Biomol. NMR 25, 1, 63-71.
    11. Wang, Q., Goh, A. M., Howley, P. M. and Walters, K. J. (2003) Ubiquitin Recognition by the DNA Repair Protein hHR23a. Biochemistry (N. Y.) 42, 13529-13535.
    12. Walters, K. J., Lech, P. J., Goh, A. M., Wang, Q. and Howley, P. M. (2003) DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a. Proc. Natl. Acad. Sci. U. S. A. 100, 12694-12699.
    13. Tianzhi Wang, Sheng Cai and Zuiderweg, E. R. P. (2003) Temperature Dependence of Anisotropic Protein Backbone Dynamics. J. Am. Chem. Soc. 125, 8639.
    14. Platt, G. W., Simpson, S. A., Layfield, R. and Searle, M. S. (2003) Stability and Folding Kinetics of a Ubiquitin Mutant with a Strong Propensity for Nonnative Beta-Hairpin Conformation in the Unfolded State. Biochemistry (N. Y.) 42, 13762-13771.
    15. Petkewich, R. (2003) Integrating micromixer and microcoils for time-resolved NMR. Anal. Chem. 75, 94.
    16. Hus, J.-C., Peti, W., Griesinger, C., Bruschweiler, R.(2003) Self-Consistency Analysis of Dipolar Couplings in Multiple Alignments of Ubiquitin. J. Am. Chem. Soc. 125, 19, 5596-5597.
    17. Meiler, J., Peti, W., Griesinger, C.(2003) Dipolar Couplings in Multiple Alignments Suggest alpha-Helical Motion in Ubiquitin. J. Am. Chem. Soc. 125, 27, 8072-8073.
    18. Paulsori, E. K., Morcombe, C. R., Gaponenko, V., Dancheck, B., Byrd, R. A. and Zilm, K. W. (2003) Sensitive High Resolution Inverse Detection NMR Spectroscopy of Proteins in the Solid State. J. Am. Chem. Soc. 125, 15831-15836.
    19. Lima, C. D. (2003) CUE'd up for Monoubiquitin. Cell 113, 554.
    20. Kitahara, R. and Akasaka, K. (2003) Close identity fo a pressure-stabilized intermediate with a kinetic intermediate in protein folding. Proc. Natl. Acad. Sci. U. S. A. 100, 3167.
    21. Kakuta, M., Jayawickrama, D. A., Wolters, A. M., Manz, A. and Sweedler, J. V. (2003) Micromixer-Based Time-Resolved NMR: Applications to Ubiquitin Protein Conformation. Anal. Chem. 75, 956.
    22. Bilodeau, P. S., Winistorfer, S. C., Kearney, W. R., Robertson, A. D. and Piper, R. C. (2003) Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome. J. Cell Biol. 163, 237-243.
    23. Sundd, M., Robertson, A. D. (Sept 2003) Rearrangement of Charge-Charge Interactions in Variant Ubiquitins as Detected by Double-Mutant Cycles and NMR. J. Mol. Biol. 332, 4, 927-936.
    24. Radley, T. L., Markowska, A. I., Bettinger, B. T., Ha, J.-H., Loh, S. N. (Sep 2003) Allosteric Switching by Mutually Exclusive Folding of Protein Domains. J. Mol. Biol. 332, 3, 529-536.

  • 2002
    1. Meier, S., Haussinger, D., Grzesiek, S. (Dec 2002) Charged acrylamide copolymer gels as media for weak alignment. J. Biomol. NMR 24, 4, 351-356.
    2. Hus, J.-C., Bruschweiler, R. (Oct 2002) Principal component method for assessing structural heterogeneity across multiple alignment media. J. Biomol. NMR 24, 2, 123-132.
    3. Flynn, P. F., Milton, M. J., Babu C.R.,Wand, A. J. (Aug 2002) A Simple and Effective NMR Cell for Studies of Encapsulated Proteins Dissolved in Low Viscosity Solvents. J. Biomol. NMR 23, 4, 311-316. BMRB Entry 5387
    4. Permi, P. (Jul 2002) Intraresidual HNCA: An experiment for correlating only intraresidual backbone resonances. J. Biomol. NMR 23, 3, 201-209.
    5. Zweckstetter, M., Bax, A. (Jun 2002) Evaluation of uncertainty in alignment tensors obtained from dipolar couplings J. Biomol. NMR 23, 2, 127-137.
    6. Mills, J. L., Szyperski, T. (May 2002) Protein dynamics in supercooled water: The search for slow motional modes. J. Biomol. NMR 23, 1, 63-67.
    7. Kloiber, K., Schuler, W., Konrat, R. (Apr 2002) Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation. J. Biomol. NMR 22, 4, 349-363.
    8. Wedemeyer, W. J., Rohl, C. A., Scheraga, H. A. (Feb 2002) Exact solutions for chemical bond orientations from residual dipolar couplings. J. Biomol. NMR 22, 2, 137-151.
    9. Giesen, A. W., Bae, L. C., Barret, C. L., Chyba, J. A. Chaykovsky, M. M., Cheng, m.-C., Myrray, J. H., Oliver, E. J., Sullivan, S. M., Brown, J. M., Homans, S. W. (Jan 2002) 1H-filtered correlation experiments for assignment and determination of coupling constants in backbone labelled proteins. J. Biomol. NMR 22, 1, 21-26.
    10. Permi, P. (Jan 2002) A spin-state-selective experiment for measuring heteronuclear one-bond and homonuclear two-bond couplings from an HSQC-type spectrum. J. Biomol. NMR 22, 1, 27-35.
    11. Haihong Sun, Sanders, L. K. and Oldfield, E. (2002) Carbon-13 NMR Shielding in the Twenty Common Amino Acids: Comparisons with Experimental Results in Proteins. J. Am. Chem. Soc. 124, 5486.
    12. Sundd, M., Iverson, N., Ibarra-Molero, B., Sanchez-Ruiz, J. M., Robertson, A. D. (2002) Electrostatic Interactions in Ubiquitin: Stabilization of Carboxylates by Lysine Amino Groups. Biochemistry 41, 24, 7586-7596.
    13. Ermolenko, D. N., Thomas, S. T., Aurora, R., Gronenborn, A. M., Makhatadz, G. I., (Sep 2002) Hydrophobic Interactions at the Ccap Position of the C-capping Motif of alpha-Helices. J. Mol. Biol. 322, 1, 123-135.
    14. Mueller, T. D., Feigon, J. (Jun 2002) Solution Structures of UBA Domains Reveal a Conserved Hydrophobic Surface for Protein-Protein Interactions. J. Mol. Biol. 319, 5, 1243-1255.
    15. Cordier, F., Grzesiek, S. (Apr 2002) Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR. J. Mol. Biol. 317, 5, 739-752.

  • 2001
    1. Andrec, M., Du, P., Levy, R. M. (Dec 2001) Protein backbone structure determination using only residual dipolar couplings from one ordering medium. J. Biomol. NMR 21, 4, 335-347.
    2. Yao, X. L., Hong, M. (Jul 2001) Dipolar filtered 1H-13C heteronuclear correlation spectroscopy for resonance assignment of proteins. J. Biomol. NMR 20, 3, 263-274.
    3. Marley, J., Lu, M., Bracken, C. (May 2001) A method for efficient isotopic labeling of recombinant proteins. J. Biomol. NMR 20, 1, 71-75.
    4. Giesen, A. W., Bae, L. C., Barret, C. L., Chyba, J. A. Chaykovsky, M. M., Cheng, M.-C., Murray, J. H., Oliver, E. J., Sullivan, S. M., Brown, J. M., Dahlquist, F. W., Homans, S. W. (Mar 2001) Measurement of one-bond 1HA-13CA couplings in backbone-labelled proteins. J. Biomol. NMR 19, 3, 255-260.
    5. Peti, W., Smith, L. J., Redfield, C., Schwalbe, H. (Feb 2001) Chemical shifts in denatured proteins: Resonance assignments for denatured ubiquitin and c omparisons with other denatured proteins. J. Biomol. NMR 19, 2, 153-165. BMRB Entry 4375
    6. Wang, C., Xi, J., Begley, T. P. and Nicholson, L. K. (2001) Solution structure of ThiS and implications for the evolutionary roots of ubiquitin. Nat. Struct. Biol. 8, 47.
    7. Juranic, N., Macura, S. (2001) Correlations among 1JNC' and h3JNC' Coupling Constants in the Hydrogen-Bonding Network of Human Ubiquitin. J. Am. Chem. Soc. 123, 17, 4099-4100.
    8. Prompers, J. J. and Bruschweiler, R. (2001) Reorientational Eigenmode Dynamics: A Combined MD/NMR Relaxation Analysis Method for Flexible.. J. Am. Chem. Soc. 123, 7305.
    9. Kitahara, R., Yamada, H. and Akasaka, K. (2001) Two Folded Conformers of Ubiquitin Revealed by High-Pressure NMR. Biochemistry (N. Y.) 40, 13556.
    10. Jourdan, M., Searle, M. S. (2001) Insights into the Stability of Native and Partially Folded States of Ubiquitin: Effects of Cosolvents and Denaturants on the Thermodynamics of Protein Folding. Biochemistry 40, 34, 10317-10325.
    11. Bolton, D., Evans, P. A., Stott, K., Broadhurst, R. W. (Dec 2001) Structure and properties of a dimeric N-terminal fragment of human ubiquitin. J. Mol. Biol. 314, 4, 773-787. BMRB Entry 5101
    12. Propers, J. J., Scheurer, C., Brushweiler, R. (Feb 2001) Characterization of NMR relaxation-active motions of a partially folded A-state analogue of ubiquitin. J. Mol. Biol. 305, 5, 1085-1097.

  • 2000
    1. Sass, H.-J., Musco, G., Stahl, S. J., Wingfield, P. T., Grzesiek, S. (Dec 2000) Solution NMR of proteins within polyacrylamide gels: Diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes. J. Biomol. NMR 18, 4, 303-309.
    2. Hamilton, K. S., Ellison, M. J., Shaw, G. S. (Dec 2000) Identification of the Ubiquitin Interfacial Residues in a Ubiquitin-E2 Covalent Complex. J. Biomol. NMR 18, 4, 319-327. BMRB Entry 4769
    3. Peti, W., Griesinger, C., Bermel, W. (Nov 2000) Adiabatic TOCSY for C,C and H,H J-transfer. J. Biomol. NMR 18, 3, 199-205.
    4. Kloiber, K., Konrat, R. (Jul 2000) Measurement of the protein backbone dihedral angle phi based on quantification of remote CSA/DD interference in inter-residue 13C'(i - 1)-13CA(i) multiple-quantum coherences. J. Biomol. NMR 17, 3, 265-268.
    5. Calomagno, T., Peti, W., Griesinger, C. (Jun 2000) A new method for the simultaneous measurement of magnitude and sign of 1DCH and 1DHH dipolar couplings in methylene groups. J. Biomol. NMR 17, 2, 99-109.
    6. Permi, P., Rosevear, P. R., Annila, A. (May 2000) A set of HNCO-based experiments for measurement of residual dipolar couplings in 15N, 13C, (2H)-labeled proteins. J. Biomol. NMR 17, 1, 43-54.
    7. Folmer, R., Otting, G. (Mar 2000) Sensitivity enhancement in (HCA)CONH experiments. J. Biomol. NMR 16, 3, 229-223.
    8. Permi, P., Kilpelainen, I, Annila, A., Heikkinen, S. (Jan 2000) Intensity modulated HSQC and HMQC: Two simple methods to measure 3JHNHA in proteins. J. Biomol. NMR 16, 1, 29-37.
    9. Jourdan, M., Griffiths-Jones, S. R. and Searle, M. S. (2000) Folding of a beta-hairpin peptide derived from the N-terminus of ubiquitin. European Journal of Biochemistry 267, 3539-3548.
    10. Thomas, S. T., Makhatadze, G. I. (2000) Contribution of the 30/36 Hydrophobic Contact at the C-Terminus of the alpha-Helix to the Stability of the Ubiquitin Molecule. Biochemistry 39, 33, 10275-10283.
    11. Peti, W., Hennig, M., Smith, L. J., Schwalbe, H. (2000) NMR Spectroscopic Investigation of Psi Torsion Angle Distribution in Unfolded Ubiquitin from Analysis of 3J(CA,CA) Coupling Constants and Cross-Correlated GammaC(HNN,CAHA) Relaxation Rates. J. Am. Chem. Soc. 122, 48, 12017-12018.
    12. Carlomagno, T., Maurer, M., Hennig, M., Griesinger, C. Ubiquitin Backbone Motion Studied via NHN-C'CA Dipolar-Dipolar and C'-C'CA/NHN CSA-Dipolar Cross-Correlated Relaxation. J. Am. Chem. Soc. 122, 21, 5105-5113.  
    13. Ferrage, F., Eykyn, T. R. and Bodenhausen, G. (2000) Coherence transfer by single-transition cross-polarization: Quantitation of cross-correlation effects in nuclear magnetic resonance. J. Chem. Phys. 113, 3, 1081-1087.

  • 1999
    1. Johnson, E. C., Handel, T. M. (Oct 1999) Effect of hydrophobic core packing on sidechain dynamics. J. Biomol. NMR 15, 2, 135-143.
    2. Johnson, E. C., Lazar, g. A., Desjarlais, J. R., Handel, T. M. (1999) Solution structure and dynamics of a designed hydrophobic core variant of ubiquitin. Structure 7, 967-976. BMRB Entry 4493
    3. Johnson, E. C., Lazar, g. A., Desjarlais, J. R., Handel, T. M. (1999) Rotamer Strain as a Determinant of Protein Structural Specificity. Protein Sci. 8, 2598-2610. BMRB Entry 4663
    4. Hong, M. (Sep 1999) Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR. J. Biomol. NMR 15, 1, 1-14.
    5. Moltke, S., Grzesiek, S. (Sep 1999) Structural constraints from residual tensorial couplings in high resolution NMR without an explicit term for the alignment tensor. J. Biomol. NMR 15, 1, 77-82.
    6. Lee, A. L., Wand, A. J. (Feb 1999) Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation. J. Biomol. NMR 13, 2, 101-112. BMRB Entry 4245
    7. Cordier, F., Dingley, A. J., Grzesiek, S. (Feb 1999) A doublet-separated sensitivity-enhanced HSQC for the determination of scalar and dipolar one-bond J-couplings. J. Biomol. NMR 13, 2, 175-180.
    8. Ottiger, M., Bax, A. (Feb 1999) Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values. J. Biomol. NMR 13, 2, 187-191.
    9. Chiarparin, E., Pelupessy, P., Cutting, B., Eykyn, T. R., Bodenhausen, G. (Jan 1999) Normalized one-dimensional NOE measurements in isotopically labeled macromolecules using two-way cross-polarization. J. Biomol. NMR 13, 1, 61-65.
    10. Finucane, M. D., Woolfson, D. N. (1999) Core-Directed Protein Design. II. Rescue of a Multiply Mutated and Destabilized Variant of Ubiquitin. Biochemistry 38, 36, 11613-11623.
    11. Sakamoto, T. and Tanaka, T. (1999) An NMR analysis of ubiquitin recognition by yeast ubiquitin hydrolase: Evidence for novel substrate recognition by a cysteine protease. Biochemistry (N. Y.) 38, 11634.
    12. Ottiger, M. and Bax, A. (1999) How tetrahedral are methyl groups in proteins? A liquid crystal NMR study. J. Am. Chem. Soc. 121, 4690.
    13. Fushman, D. and Tjandra, N. (1999) An approach to direct determination of protein dynamics from 15N NMR relaxation at multiple fields, independent of variable 15N chemical shift anisotropy and chemical exchange contributions. J. Am. Chem. Soc. 121, 8577.
    14. Wilkinson, K. D., Laleli-Sahin, E., Urbauer, J., Larsen, C. N., Shih, G. H., Haas, A. L., Walsh, S. T. R., Wand, A. J. (Sep 1999) The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3. J. Mol. Biol. 291, 5, 1067-1077.
    15. Miura, T., Klaus, W. Gsell, B., Miyamoto, C., Senn, H. (Jul 1999) Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution. J. Mol. Biol. 290, 1, 213-228.

  • 1998
    1. Yang, D., Tolman, J. R., Goto, N. K., Kay, L. E. (Aug 1998) An HNCO-based Pulse Scheme for the Measurement of 13CA-1HA; One-bond Dipolar couplings in 15N, 13C Labeled Proteins. J. Biomol. NMR 12, 2, 325-332.
    2. Straus, S. K., Bermi, T., Ernst, R. R., (Jul 1998) Experiments and strategies for the assignment of fully13 C/15N-labelled polypeptides by solid state NMR. J. Biomol. NMR 12, 1, 39-50.
    3. Astrof, N., Bracken, C., Cavanagh, J., Palmer, A. G, III (May 1998) CO_H(N)CACB experiments for assigning backbone resonances in ^13C/^15N-labeled proteins. J. Biomol. NMR 11, 4, 451-456.
    4. Hu, J.-S., Bax, A. (Feb 1998) Measurement of Three-bond, 13C'-13C? J Couplings in Human Ubiquitin by a Triple. J. Biomol. NMR 11, 2, 199-203.
    5. Ottiger, M., Bax, A. (Feb 1998) Determination of Relative N-HN, N-C', CA-C', and CA-HA Effective Bond Lengths in a Protein by NMR in a Dilute Liquid Crystalline Phase J. Am. Chem. Soc. 120, 47, 12334-12341
    6. Lienin, S. F.; Bremi, T.; Brutscher, B., Bruschweiler, R., Ernst, R. R. (1998) Anisotropic Intramolecular Backbone Dynamics of Ubiquitin Characterized by NMR Relaxation and MD Computer Simulation. J. Am. Chem. Soc. 120, 39, 870-9879.
    7. Fushman, D., Cowburn, D. (1998) Model-Independent Analysis of 15N Chemical Shift Anisotropy from NMR Relaxation Data. Ubiquitin as a Test Example. J. Am. Chem. Soc. 120, 28, 7109-7110.
    8. Cornilescu, G., Marquardt, J., L., Ottiger, M., Bax, A. (1998) Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase. J. Am. Chem. Soc. 120, 6836-6837.

  • 1997
    1. Theis, K., Dingley, A. J., Hoffman, A., Omichinski, J. G., Grzesiek, S. (Dec 1997) Determination of backbone nitrogen-nitrogen J correlations in proteins. J. Biomol. NMR 10, 4, 403-408.
    2. Bax, A., Tjandra, N. (Oct 1997) High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium. J. Biomol. NMR 10, 3 289-292.
    3. Huang, K., Andrec, M., Heald, S., Blake, P., Prestegard, J. H. (Jul 1997) Performance of a neural-network-based determination of amino acid class and secondary structure from 1H-15N NMR data. J. Biomol. NMR 10, 1, 45-52.
    4. Lee, L. K., Rance, M., Chazin, W. J., Palmer, A. G. III (Apr 1997) Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13CA nuclear spin relaxation. J. Biomol. NMR 9, 3, 287-298.
    5. Hu, J.-S., Bax, A. (Apr 1997) X1 angle information from a simple two-dimensional NMR experiment that identifies trans 3JNC? couplings in isotopically enriched proteins. J. Biomol. NMR 9, 3, 323-328.
    6. Grzesiek, S., Bax, A. (Feb 1997) A three-dimensional NMR experiment with improved sensitivity for carbonyl-carbonyl J correlation in proteins. J. Biomol. NMR 9, 2, 207-211.
    7. Bracken, C., Palmer, A. G. III, Cavanagh, J. (Jan 1997) (H)N(COCA)NH and HN(COCA)NH experiments for 1H-15N backbone assignments in 13C/15N-labeled proteins. J. Biomol. NMR 9, 1, 94-100.
    8. Tjandra, N. and Bax, A. (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline med. Science 278, 1111.
    9. Service, R. F. (1997) Lining up proteins for NMR. Science 278, 1015.
    10. Brutscher, B., Bruschweiler, R., Ernst, R. R. (1997) Backbone Dynamics and Structural Characterization of the Partially Folded A State of Ubiquitin by 1H, 13C, and 15N Nuclear Magnetic Resonance Spectroscopy. Biochemistry 36, 42, 13043-13053.
    11. Ottiger, M., Bax, A. (Feb 1997) An Empirical Correlation between Amide Deuterium Isotope Effects on 13CA Chemical Shifts and Protein Backbone Conformation. J. Am. Chem. Soc. 119, 34, 8070-8075.

  • PRE-1997
    1. Wand, A. J., Urbauer, J. L., Robert P. McEvoy, R. P., and Bieber, R. J. (1996) Internal Dynamics of Human Ubiquitin Revealed by 13C-Relaxation Studies of Randomly Fractionally Labeled Protein. Biochemistry (N. Y.) 35(19) pp 6116 - 6125.
    2. LiWang, A. C. and Bax, A. (1996) Equilibrium Protium/Deuterium Fractionation of Backbone Amides in U--13C/15N Labeled Human Ubiquitin by Triple Resonance NMR. J. Am. Chem. Soc. 118, 12864-12865.
    3. Tjandra, N., Grzesiek, S., Bax, A. (1996) Magnetic Field Dependence of Nitrogen-Proton J Splittings in 15N-Enriched Human Ubiquitin Resulting from Relaxation Interference and Residual Dipolar Coupling. J. Am. Chem. Soc. 118, 26, 6264-6272.
    4. Wang, A. C., Bax, A.(1996) Determination of the Backbone Dihedral Angles in Human Ubiquitin from Reparametrized Empirical Karplus Equations J. Am. Chem. Soc. 118, 10, 2483-2494.
    5. Tjandra, N. and Feller, S. E., Pastor, R. W., Bax, A. (1995) Rotational diffusion anisotropy of human ubiquitin from 15N NMR relaxation. J. Am. Chem. Soc. 117, 50, 12562.
    6. Wang, A. C., Bax, A. (1995) Reparametrization of the Karplus Relation for 3J(H.alpha.-N) and 3J(HN-C') in Peptides from Uniformly 13C/15N-Enriched Human Ubiquitin J. Am. Chem. Soc. 117, 6, 1810-1813.
    7. Abseher, R., Ludemann, S., Schrieber, H., Steinhauser, O. (Jun 1995) NMR Cross-relaxation Investigated by Molecular Dynamics Simulation: A Case Study of Ubiquitin in Solution. J. Mol. Biol. 249, 3, 604-624.
    8. Denisov, V. P., Halle, B. (Feb 1995) Protein Hydration Dynamics in Aqueous Solution: A Comparison of Bovine Pancreatic Trypsin Inhibitor and Ubiquitin by Oxygen-17 Spin Relaxation Dispersion. J. Mol. Biol. 245, 5, 682-697.
    9. Denisov, V. P., Halle, B. (Feb 1995) Hydrogen Exchange and Protein Hydration: The Deuteron Spin Relaxation Dispersions of Bovine Pancreatic Trypsin Inhibitor and Ubiquitin. J. Mol. Biol. 249, 3, 698-709.
    10. Cox, J. P. L., Evans, P. A., Packman, L. C., Williams, D. H., Woolfson, D. N. (Nov 1993) Dissecting the Structure of a Partially Folded Protein : Circular Dichroism and Nuclear Magnetic Resonance Studies of Peptides from Ubiquitin. J. Mol. Biol. 234, 2, 438-492.
    11. Woolfson, D. N., Cooper, A., Harding, M. M., Williams, D. H., Evans, P. A. (Jan 1993) Protein Folding in the Absence of the Solvent Ordering Contribution to the Hydrophobic Interaction. J. Mol. Biol. 229, 2, 502-511.
    12. Khorasanizadeh, S., Peters, I. D., Butt, T. R., Roder, (1993) Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry 32, 27, 7054-7063.
    13. Pan, Y., Briggs, M. S. (1992) Hydrogen exchange in native and alcohol forms of ubiquitin. Biochemistry 31, 46, 11405-11412.
    14. Schneider, D. M., Dellwo, M. J., Wand, A. J. (1992) Fast internal main-chain dynamics of human ubiquitin. Biochemistry 31, 46, 3645-3652. BMRB Entries 2573 2574
    15. Harding, M. M., Williams, D. H., Woolfson, D. N. (1991) Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin. Biochemistry 30, 12, 3120-3128. BMRB Entry 1520
    16. Weber, P. L., Brown, S. C. and Mueller, L. (1987) Sequential Proton Nmr Assignments and Secondary Structure Identification of Human Ubiquitin. Biochemistry (N. Y.) 26, 7282-7290. BMRB Entry 68
    17. Saus, J. and Timoneda, J. (1987) Atp-Dependent Degradation of Iodine-125 Bovine Serum Albumin by Rabbit Reticulocytes does Not Need Repression of an Endogenous Inhibitor. Physiol. Chem. Phys. Med. NMR 19, 51-58.
    18. Ecker, D. J., Butt, T. R., Marsh, J., Sternberg, E. J., Margolis, N., Monia, B. P., Jonnalagadda, S., Khan, M. I., Weber, P. L. and Et, A. (1987) Gene Synthesis Expression Structures and Functional Activities of Site -Specific Mutants of Ubiquitin. J. Biol. Chem. 262, 14213-14221.
    19. Di Stefano, D. L. and Wand, A. J. (1987) Two-Dimensional Proton Nmr Study of Human Ubiquitin a Main Chain Directed Assignment and Structure Analysis. Biochemistry (N. Y.) 26, 7272-7281.
    20. Krishna, N. R., Huang, D. H., Vaughn, J. B.,Jr, Heavner, G. A. and Goldstein, G. (1981) Proton Nmr Study of an Active Penta Peptide Fragment of Ubiquitin. Biochemistry (N. Y.) 20, 3933-3940.
    21. Cary, P. D., King, D. S., Crane, R. C., Bradbury, E. M., Rabbani, A., Goodwin, G. H. and Johns, E. W. (1980) Structural Studies on 2 High Mobility Group Proteins from Calf Thymus Hmg -14 and Hmg-20 Ubiquitin and their Interaction with Dna. European Journal of Biochemistry 112, 577-588.
    22. Lenkinski, R. E., Chen, D. M., Glickson, J. D. and Goldstein, G. (1977) Nmr Studies of the Denaturation of Ubiquitin. Biochim. Biophys. Acta 494, 126-130.