Solution NMR spectroscopy beyond 25 kDa.

Improvements in NMR instrumentation, higher magnetic field strengths, novel NMR experiments and new deuterium-labeling strategies have significantly increased the scope of structural problems that can now be addressed by solution NMR methods. To date, a number of structures of proteins of 30 kDa have been solved using multidimensional 15N,13C,2H NMR techniques, and this molecular weight limit will probably be surpassed in the near future.

[1]  K. Wüthrich NMR of proteins and nucleic acids , 1988 .

[2]  O. Jardetzky,et al.  The solution structures of the trp repressor-operator DNA complex. , 1994, Journal of molecular biology.

[3]  S. Grzesiek,et al.  Two-Dimensional NMR Methods for Determining χ1 Angles of Aromatic Residues in Proteins from Three-Bond JC‘Cγ and JNCγ Couplings , 1997 .

[4]  B. Farmer,et al.  Assignment of aliphatic side-chain 1HN/15N resonances in perdeuterated proteins , 1996, Journal of biomolecular NMR.

[5]  S. Opella,et al.  Three-dimensional solid-state NMR experiment that correlates the chemical shift and dipolar coupling frequencies of two heteronuclei. , 1995, Journal of Magnetic Resonance - Series B.

[6]  Ad Bax,et al.  Multidimensional nuclear magnetic resonance methods for protein studies , 1994 .

[7]  Angela M. Gronenborn,et al.  The Impact of Direct Refinement against 13Cα and 13Cβ Chemical Shifts on Protein Structure Determination by NMR , 1995 .

[8]  T Pawson,et al.  Selective methyl group protonation of perdeuterated proteins. , 1996, Journal of molecular biology.

[9]  J. Chattopadhyaya,et al.  The differences in the T2 relaxation rates of the protons in the partially-deuteriated and fully protonated sugar residues in a large oligo-DNA ('NMR-window') gives complementary structural information. , 1994, Nucleic acids research.

[10]  Y. Kyōgoku,et al.  An efficient HN(CA)NH pluse scheme for triple-resonance 4D correlation of sequential amide protons and nitrogens-15 in deuterated proteins. , 1997, Journal of magnetic resonance.

[11]  K. Constantine,et al.  Localizing the NADP+ binding site on the MurB enzyme by NMR , 1996, Nature Structural Biology.

[12]  Weontae Lee,et al.  A Suite of Triple Resonance NMR Experiments for the Backbone Assignment of 15N, 13C, 2H Labeled Proteins with High Sensitivity , 1994 .

[13]  Ad Bax,et al.  Four-Dimensional 15N-Separated NOESY of Slowly Tumbling Perdeuterated 15N-Enriched Proteins. Application to HIV-1 Nef , 1995 .

[14]  L. Kay,et al.  An HNCA Pulse Scheme for the Backbone Assignment of 15N,13C,2H-Labeled Proteins: Application to a 37-kDa Trp Repressor-DNA Complex , 1994 .

[15]  S. Grzesiek,et al.  Carbon-13 line narrowing by deuterium decoupling in deuterium/carbon-13/nitrogen-15 enriched proteins. Application to triple resonance 4D J connectivity of sequential amides , 1993 .

[16]  A. Bax,et al.  Determination of φ and χ1 Angles in Proteins from 13C−13C Three-Bond J Couplings Measured by Three-Dimensional Heteronuclear NMR. How Planar Is the Peptide Bond? , 1997 .

[17]  J H Prestegard,et al.  Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[18]  B. Farmer,et al.  ASSIGNMENT OF SIDE-CHAIN 13C RESONANCES IN PERDEUTERATED PROTEINS , 1995 .

[19]  A. Palmer,et al.  Dynamic properties of proteins from NMR spectroscopy. , 1993, Current opinion in biotechnology.

[20]  A. Petros,et al.  Structure and ligand recognition of the phosphotyrosine binding domain of Shc , 1995, Nature.

[21]  J. Prestegard,et al.  A quantitative J-correlation experiment for the accurate measurement of one-bond amide 15N-1H couplings in proteins. , 1996, Journal of magnetic resonance. Series B.

[22]  Improved large scale culture of Methylophilus methylotrophus for 13C/15N labeling and random fractional deuteration of ribonucleotides. , 1996, Nucleic acids research.

[23]  J. Williamson,et al.  Preparation of Specifically Deuterated RNA for NMR Studies Using a Combination of Chemical and Enzymatic Synthesis , 1996 .

[24]  E. Kupče,et al.  Use of selective C alpha pulses for improvement of HN(CA)CO-D and HN(COCA)NH-D experiments. , 1996, Journal of magnetic resonance. Series B.

[25]  F. Dahlquist,et al.  Large modular proteins by NMR , 1997, Nature Structural Biology.

[26]  P. Hajduk,et al.  Discovering High-Affinity Ligands for Proteins: SAR by NMR , 1996, Science.

[27]  D. S. Garrett,et al.  Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system. , 1997, Biochemistry.

[28]  C. Gayathri,et al.  Dipolar magnetic field effects in NMR spectra of liquids , 1982 .

[29]  P. Domaille,et al.  An Approach to the Structure Determination of Larger Proteins Using Triple Resonance NMR Experiments in Conjunction with Random Fractional Deuteration , 1996 .

[30]  Jean M. Severin,et al.  Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance , 1997, Nature Structural Biology.

[31]  L. Kay,et al.  An (H)C(CO)NH-TOCSY pulse scheme for sequential assignment of protonated methyl groups in otherwise deuterated 15N, 13C-labeled proteins , 1996, Journal of biomolecular NMR.

[32]  Jack Greenblatt,et al.  Methods for Measurement of Intermolecular NOEs by Multinuclear NMR Spectroscopy: Application to a Bacteriophage λ N-Peptide/boxB RNA Complex , 1997 .

[33]  O Jardetzky,et al.  Refined solution structures of the Escherichia coli trp holo- and aporepressor. , 1993, Journal of molecular biology.

[34]  K. Constantine,et al.  Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes. , 1997, Journal of molecular biology.

[35]  J. Prestegard,et al.  NMR evidence for slow collective motions in cyanometmyoglobin , 1997, Nature Structural Biology.

[36]  R. Meadows,et al.  X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death , 1996, Nature.

[37]  F. Richards,et al.  NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation. , 1988, Biochemistry.

[38]  G. L. Kenyon,et al.  Studies of macromolecular structure by 13 C nuclear magnetic resonance. II. A specific labeling approach to the study of histidine residues in proteins. , 1973, Journal of the American Chemical Society.

[39]  H. Li,et al.  A sensitive HN(CA)CO experiment for deuterated proteins. , 1996, Journal of magnetic resonance. Series B.

[40]  V Dötsch,et al.  Amino-acid-type identification for deuterated proteins with a beta-carbon-edited HNCOCACB experiment. , 1996, Journal of magnetic resonance. Series B.

[41]  S. Grzesiek,et al.  Spin-locked multiple quantum coherence for signal enhancement in heteronuclear multidimensional NMR experiments , 1995, Journal of Biomolecular NMR.

[42]  Eric Oldfield,et al.  Chemical shifts and three-dimensional protein structures , 1995, Journal of biomolecular NMR.

[43]  M. Hennig,et al.  Direct measurement of angles between bond vectors in high-resolution NMR. , 1997, Science.

[44]  R. Meadows,et al.  Structure of Bcl-xL-Bak Peptide Complex: Recognition Between Regulators of Apoptosis , 1997, Science.

[45]  L. Kay,et al.  Assignment of 15N, 13Cα, 13Cβ, and HN Resonances in an 15N,13C,2H Labeled 64 kDa Trp Repressor−Operator Complex Using Triple-Resonance NMR Spectroscopy and 2H-Decoupling , 1996 .

[46]  M. Wittekind,et al.  Incorporation of 1H/13C/15N-{Ile, Leu, Val} into a Perdeuterated, 15N-Labeled Protein: Potential in Structure Determination of Large Proteins by NMR , 1996 .

[47]  L. Kay Field gradient techniques in NMR spectroscopy. , 1995, Current opinion in structural biology.

[48]  M. Kainosho,et al.  C5′ Methylene Proton Signal Assignment of DNA/RNA Oligomers Labeled with C5′‐Monodeuterated Nucleosides by 1H–31P HSQC Spectroscopy , 1996 .

[49]  H. Crespi,et al.  Proton Magnetic Resonance of Proteins Fully Deuterated except for 1H-Leucine Side Chains , 1968, Science.

[50]  D. S. Garrett,et al.  Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. , 1997, Biochemistry.

[51]  L. Kay,et al.  Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR. , 1997, Biochemistry.

[52]  B. Farmer,et al.  Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II. , 1996, Journal of molecular biology.

[53]  D. Shortle,et al.  Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. , 1997, Journal of molecular biology.

[54]  Ad Bax,et al.  Magnetic Field Dependence of Nitrogen−Proton J Splittings in 15N-Enriched Human Ubiquitin Resulting from Relaxation Interference and Residual Dipolar Coupling , 1996 .

[55]  D. Wishart,et al.  The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data , 1994, Journal of biomolecular NMR.

[56]  R. Tycko Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteins , 1996, Journal of biomolecular NMR.

[57]  A. Bax,et al.  Measurement of dipolar contributions to 1JCH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra. , 1997, Journal of magnetic resonance.

[58]  G. Marius Clore,et al.  Use of dipolar 1H–15N and 1H–13C couplings in the structure determination of magnetically oriented macromolecules in solution , 1997, Nature Structural Biology.

[59]  Bennett T. Farmer,et al.  Use of 1HN-1HN NOEs to Determine Protein Global Folds in Perdeuterated Proteins , 1995 .

[60]  Lewis E. Kay,et al.  Production and Incorporation of 15N, 13C, 2H (1H-δ1 Methyl) Isoleucine into Proteins for Multidimensional NMR Studies , 1997 .

[61]  S. Teichmann,et al.  An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residue types , 1996, Journal of biomolecular NMR.

[62]  G. Wagner,et al.  Effect of deuteration on the amide proton relaxation rates in proteins. Heteronuclear NMR experiments on villin 14T. , 1994, Journal of magnetic resonance. Series B.

[63]  O. Jardetzky,et al.  High-Resolution Nuclear Magnetic Resonance Spectra of Selectively Deuterated Staphylococcal Nuclease , 1968, Science.

[64]  R. Griffey,et al.  Proton-detected heteronuclear edited and correlated nuclear magnetic resonance and nuclear Overhauser effect in solution , 1987, Quarterly Reviews of Biophysics.

[65]  D. S. Garrett,et al.  Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy , 1997, Nature Structural Biology.

[66]  M. Shirakawa,et al.  The use of heteronuclear cross-polarization for backbone assignment of 2H-, 15N- and 13C-labeled proteins: A pulse scheme for triple-resonance 4D correlation of sequential amide protons and 15N , 1995, Journal of biomolecular NMR.

[67]  A M Gronenborn,et al.  Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids. , 1997, Journal of magnetic resonance.

[68]  A. Bax,et al.  Delineation of .alpha.-helical domains in deuteriated Staphylococcal nuclease by 2D NOE NMR spectroscopy , 1988 .