Method for two--eld nuclear magnetic resonance measurement ,
Protein Dynamics from Nuclear Magnetic Relaxation, Chem. Soc. Rev, pp.10-1039, 2016. ,
Recovering Invisible Signals by Two-Field NMR Spectroscopy, Angewandte Chemie International Edition ,
Side-EEects of Cross-Polarization Enhanced Dissolution DNP of Deuterated Molecules ,
Nuclear Magnetic Resonance Spectroscopy ,
URL : https://hal.archives-ouvertes.fr/cea-01393871
Study of Protein Motions by High-Resolution Relaxometry Book chapter invited contribution, work in progress ? "Full broadband carbon-13 correlations with two--eld NMR spectroscopy ,
Replication across Template T/U by Human DNA Polymerase-??, Structure, vol.17, issue.7, pp.974-980 ,
DOI : 10.1016/j.str.2009.04.011
URL : http://doi.org/10.1016/j.str.2009.04.011
Solution structure of the N-terminal domain of Bacillus subtilis ? subunit of RNA polymerase and its classiication based on structural homologs, Proteins: Structure, Function, and Bioinformatics, p.NA?NA, 2010. ,
The revolution will not be crystallized: a new method sweeps through structural biology, Nature, vol.525, issue.7568, pp.172-174 ,
DOI : 10.1038/525172a
Conformational entropy in molecular recognition by proteins, Nature, vol.10, issue.7151, pp.325-329 ,
DOI : 10.1038/nature05959
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4156320
Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR, Cell, vol.131, issue.4, pp.756-769 ,
DOI : 10.1016/j.cell.2007.09.039
Principles of Nuclear Magnetic Resonance in One and Two Dimensions. International Series of Monographs on Chemistry, 1990. ,
Cycling Li-O2 batteries via LiOH formation and decomposition, Science, vol.117, issue.32, pp.350530-533 ,
DOI : 10.1149/1.3507922
URL : https://www.repository.cam.ac.uk/bitstream/1810/253469/1/Liu-et-al%202015%20Science.pdf
DNP-Hyperpolarized 13C Magnetic Resonance Metabolic Imaging for Cancer Applications, Applied Magnetic Resonance, vol.56, issue.3-4, pp.3-4533 ,
DOI : 10.1007/s00723-008-0136-2
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2829774
Using NMR to study full intact wine bottles, Journal of Magnetic Resonance, vol.161, issue.1, pp.91-98 ,
DOI : 10.1016/S1090-7807(02)00177-5
URL : http://chemgroups.ucdavis.edu/~augustine/papers/2002_Using NMR to study full intact wine bottles.pdf
Image Formation by Induced Local Interactions: Examples Employing Nuclear Magnetic Resonance, Nature, vol.178, issue.5394, pp.190-191 ,
DOI : 10.1038/242190a0
The way to NMR structures of proteins, Nature, vol.8, issue.11, pp.923-925, 2001. ,
Protein dynamics from nuclear magnetic relaxation, Chem. Soc. Rev., vol.104, issue.9, 2016. ,
DOI : 10.1039/C5CS00832H
URL : https://hal.archives-ouvertes.fr/hal-01366187
High-resolution NMR field-cycling device for full-range relaxation and structural studies of biopolymers on a shared commercial instrument, Journal of Biomolecular NMR, vol.50, issue.2, pp.159-177 ,
DOI : 10.1007/s10858-011-9594-1
Nanosecond Time Scale Motions in Proteins Revealed by High-Resolution NMR Relaxometry, Journal of the American Chemical Society, vol.135, issue.49, pp.18665-18672 ,
DOI : 10.1021/ja409820g
URL : http://doi.org/10.1021/ja409820g
Rotational diffusion anisotropy of human ubiquitin from 15N NMR relaxation, Journal of the American Chemical Society, vol.117, issue.50, pp.12562-12566 ,
DOI : 10.1021/ja00155a020
Anisotropic Intramolecular Backbone Dynamics of Ubiquitin Characterized by NMR Relaxation and MD Computer Simulation, Journal of the American Chemical Society, vol.120, issue.38, pp.9870-9879, 1998. ,
DOI : 10.1021/ja9810179
A Thorough Dynamic Interpretation of Residual Dipolar Couplings in Ubiquitin, Journal of Biomolecular NMR, vol.34, issue.2, pp.101-115 ,
The Principles of nuclear magnetism, 1961. ,
Protein NMR relaxation: theory, applications and outlook, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.33, pp.3-4207 ,
NMR studies of Brownian tumbling and internal motions in proteins, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.38, issue.3, pp.197-266 ,
DOI : 10.1016/S0079-6565(00)00028-5
Spin Dynamica, 2015. ,
Bloch-Redfield-Wangsness theory engine implementation using symbolic processing software, Journal of Magnetic Resonance, vol.184, issue.2, pp.196-206 ,
DOI : 10.1016/j.jmr.2006.09.023
URL : http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.573.5968
Deriving quantitative dynamics information for proteins and RNAs using ROTDIF with a graphical user interface, Journal of Biomolecular NMR, vol.128, issue.35, pp.333-352 ,
DOI : 10.1007/s10858-013-9791-1
Density and viscosity of deuterium oxide solutions from 5-70. deg, Journal of Chemical & Engineering Data, vol.16, issue.1, pp.85-87, 1971. ,
Probing Side-Chain Dynamics in Proteins by the Measurement of Nine Deuterium Relaxation Rates Per Methyl Group, The Journal of Physical Chemistry B, vol.116, issue.1, pp.606-620 ,
DOI : 10.1021/jp209304c
DRAM: Efficient adaptive MCMC, Statistics and Computing, vol.18, issue.2, pp.339-354 ,
DOI : 10.1007/s11222-006-9438-0
URL : http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.467.9433
Four-Dimensional NMR Spectroscopy of a 723-Residue Protein:?? Chemical Shift Assignments and Secondary Structure of Malate Synthase G, Journal of the American Chemical Society, vol.124, issue.34, pp.10025-10035 ,
DOI : 10.1021/ja0205636
Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy, Journal of Magnetic Resonance (1969), vol.53, issue.3, pp.521-528, 1969. ,
DOI : 10.1016/0022-2364(83)90226-3
Rapid Identification of Common Hexapyranose Monosaccharide Units by a Simple TOCSY Matching Approach, Chemistry - A European Journal, vol.230, issue.29, pp.8869-8878 ,
DOI : 10.1002/chem.200801081
Sensitivity Improvement in Isotropic Mixing (TOCSY) Experiments, Journal of Magnetic Resonance, vol.88, pp.72-85, 1990. ,
Use of zero-quantum coherences to measure high resolution n.m.r. spectra in inhomogeneous magnetic elds, Journal of the Chemical Society, Chemical Communications, issue.1, p.44, 1986. ,
NMR study of hindered rotation in 1-aryl-3,3-dimethyltriazenes, Tetrahedron, vol.24, issue.10, pp.3899-3906 ,
DOI : 10.1016/S0040-4020(01)92598-0
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy, Nature Structural Biology, vol.8, issue.4, pp.334-338, 2001. ,
DOI : 10.1038/86214
Irwin Allan Rose (1926???2015), Nature, vol.523, issue.7562, pp.532-532, 1926. ,
DOI : 10.1038/523532a
Intrinsic dynamics of an enzyme underlies catalysis, Nature, issue.7064, pp.438117-121 ,
How Emil Fischer was Led to the Lock and Key Concept for Enzyme Specificity11Presented at the symposium ???Emil Fischer: 100 Years of Carbohydrate Chemistry,??? 203rd National Meeting of the American Chemical Society, Division of Carbohydrate Chemistry, San Francisco, California, April 5???10, 1992., Adv Carbohydr Chem Biochem, vol.50, pp.1-20, 1994. ,
DOI : 10.1016/S0065-2318(08)60149-3
A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis, Nature, vol.178, issue.4610, pp.181662-666 ,
DOI : 10.1002/hlca.19490320118
Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 ???. Resolution, Nature, vol.178, issue.4711, pp.185422-427 ,
DOI : 10.1107/S0365110X5900007X
Structural basis for the suppression of skin cancers by DNA polymerase ??, Nature, vol.54, issue.7301, pp.1039-1043 ,
DOI : 10.1038/nature09104
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm, Journal of molecular biology, vol.293, issue.2, pp.321-331, 1999. ,
NMR Analysis of Viral Protein Structures, Plant Virology Protocols, pp.441-462, 2008. ,
DOI : 10.1007/978-1-59745-102-4_30
Magic-angle-spinning NMR spectroscopy of gels, Journal of Magnetic Resonance, vol.81, issue.1, pp.217-219, 1969. ,
Atomic model of the type III secretion system needle, Nature, vol.309, pp.2012-2017 ,
DOI : 10.1038/nature11079
Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy, Nature Protocols, vol.1, issue.2, pp.749-754 ,
DOI : 10.1007/s10858-005-2614-2
Développement de stratégies de marquage isotopique des groupements méhyles pour l'éude d'assemblages protéques de grande taille par RMN, pp.2014-2023 ,
Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins, Journal of Biomolecular NMR, vol.59, issue.3, pp.251-262 ,
DOI : 10.1007/s10858-013-9785-z
URL : https://hal.archives-ouvertes.fr/hal-01101628
Speeding Up Three-Dimensional Protein NMR Experiments to a Few Minutes, Journal of the American Chemical Society, vol.128, issue.28, pp.9042-9043 ,
DOI : 10.1021/ja062025p
Applications of high dimensionality experiments to biomolecular NMR, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.90, issue.91, pp.90-9149 ,
DOI : 10.1016/j.pnmrs.2015.07.001
Multiple-Quantum Magic-Angle Spinning NMR: A New Method for the Study of Quadrupolar Nuclei in Solids, Journal of the American Chemical Society, vol.117, issue.51, pp.12779-12787, 1995. ,
DOI : 10.1021/ja00156a015
NMR of proteins and nucleic acids. The George Fisher Baker non-resident lectureship in chemistry at Cornell University, 1986. ,
NMR analysis of a 900K GroEL???GroES complex, Nature, vol.24, issue.6894, pp.207-211 ,
DOI : 10.1038/7573
HNCA+, HNCO+, and HNCACB+ experiments: improved performance by simultaneous detection of orthogonal coherence transfer pathways, Journal of Biomolecular NMR, vol.239, issue.1, pp.1-9 ,
DOI : 10.1007/s10858-014-9847-x
URL : https://hal.archives-ouvertes.fr/hal-01321280
Protein structure determination from NMR chemical shifts, Proceedings of the National Academy of Sciences, pp.9615-9620 ,
DOI : 10.1016/S0022-2836(03)00021-4
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1887584
High-Resolution 3D Structure Determination of Kaliotoxin by Solid-State NMR Spectroscopy, PLoS ONE, vol.440, issue.6, pp.2359-2008 ,
DOI : 10.1371/journal.pone.0002359.s003
Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution, Proc. Natl. Acad. Sci. USA, pp.12366-12371, 1997. ,
DOI : 10.1007/BF02192855
C NMR Spectroscopy, Journal of the American Chemical Society, vol.126, issue.15, pp.4921-4925 ,
DOI : 10.1021/ja039732s
Probing Slow Dynamics in High Molecular Weight Proteins by Methyl-TROSY NMR Spectroscopy: Application to a 723-Residue Enzyme, Journal of the American Chemical Society, vol.126, issue.12, pp.3964-3973 ,
Insights into Superconducting Ultra High Field Magnet Technology, pp.2015-2019 ,
Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity, Journal of the American Chemical Society, vol.104, issue.17, pp.4546-4559, 1982. ,
DOI : 10.1021/ja00381a009
Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins, Journal of the American Chemical Society, vol.112, issue.12, pp.1124989-4991, 1990. ,
DOI : 10.1021/ja00168a070
Backbone Dynamics ofEscherichia coliRibonuclease HI: Correlations with Structure and Function in an Active Enzyme, Journal of Molecular Biology, vol.246, issue.1, pp.144-163 ,
DOI : 10.1006/jmbi.1994.0073
Mapping of Spectral Density Functions Using Heteronuclear NMR Relaxation Measurements, Journal of Magnetic Resonance, vol.98, pp.308-332, 1992. ,
Field-cycling NMR relaxometry, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.44, issue.3-4, pp.257-320 ,
DOI : 10.1016/j.pnmrs.2004.03.002
A compact high-speed mechanical sample shuttle for field-dependent high-resolution solution NMR, Journal of Magnetic Resonance, vol.214, pp.302-308 ,
DOI : 10.1016/j.jmr.2011.12.001
Mesodynamics in the SARS nucleocapsid measured by NMR field cycling, Journal of Biomolecular NMR, vol.357, issue.1-2, pp.217-225 ,
DOI : 10.1007/s10858-009-9347-6
Comparison of Solid-State Dipolar Couplings and Solution Relaxation Data Provides Insight into Protein Backbone Dynamics, Journal of the American Chemical Society, vol.132, issue.14, pp.5015-5017 ,
DOI : 10.1021/ja100645k
Cross-Relaxation in NMR Spectroscopy, Journal of the American Chemical Society, vol.128, issue.34, pp.11072-11078 ,
DOI : 10.1021/ja0600577
URL : https://hal.archives-ouvertes.fr/hal-00103657
High-level 2H/13C/15N labeling of proteins for NMR studies, Journal of Biomolecular NMR, vol.5, issue.4, pp.339-344, 1995. ,
DOI : 10.1007/BF00182275
Solution NMR-derived global fold of a monomeric 82-kDa enzyme, Proceedings of the National Academy of Sciences, vol.8, issue.1, pp.622-627 ,
DOI : 10.1016/0263-7855(96)00009-4
N-Labeled Sample, Journal of the American Chemical Society, vol.119, issue.5, pp.872-880 ,
DOI : 10.1021/ja962945f
Optimal isotope labelling for NMR protein structure determinations, Nature, vol.30, issue.7080, pp.52-57 ,
DOI : 10.1038/nature04525
Differential isotope-labeling for Leu and Val residues in a protein by E. coli cellular expression using stereo-specifically methyl labeled amino acids, Journal of Biomolecular NMR, vol.335, issue.3, pp.237-249 ,
DOI : 10.1007/s10858-013-9784-0
C Labeling Strategy Reveals a Range of Aromatic Side Chain Motion in Calmodulin, Journal of the American Chemical Society, vol.135, issue.26, pp.9560-9563 ,
DOI : 10.1021/ja4001129
??-Ketoacids as precursors for phenylalanine and tyrosine labelling in cell-based protein overexpression, Journal of Biomolecular NMR, vol.121, issue.4, pp.327-331 ,
DOI : 10.1007/s10858-013-9796-9
C-Labeled Methyl Groups, Journal of the American Chemical Society, vol.122, issue.33, pp.7898-7904 ,
DOI : 10.1021/ja000350l
Dynamic Regulation of Archaeal Proteasome Gate Opening As Studied by TROSY NMR, Science, vol.27, issue.5, pp.98-102 ,
DOI : 10.1016/j.molcel.2007.06.033
The Dynamical Theory of Nuclear Induction, Physical Review, vol.89, issue.4, pp.728-739, 1953. ,
DOI : 10.1103/PhysRev.89.728
On the Theory of Relaxation Processes, IBM Journal of Research and Development, vol.1, issue.1, pp.19-31, 1957. ,
DOI : 10.1147/rd.11.0019
Internal motions in proteins and interference effects in nuclear magnetic resonance, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.41, issue.3-4, pp.305-324, 2002. ,
DOI : 10.1016/S0079-6565(02)00051-1
Formal Theory of Spin???Lattice Relaxation, Journal of Magnetic Resonance, vol.149, issue.2, pp.160-187 ,
DOI : 10.1006/jmre.2000.2239
Nuclear spin relaxation in liquids: theory, experiments, and applications . Number 2 in Series in chemical physics, 2006. ,
DOI : 10.1201/9781420012194
URL : https://repozitorij.uni-lj.si/Dokument.php?id=39829
Nuclear spin relaxation in isotropic and anisotropic media, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.57, issue.2, pp.111-158 ,
DOI : 10.1016/j.pnmrs.2010.04.003
URL : https://hal.archives-ouvertes.fr/hal-00605407
Rotations and angular moments in quantum mechanics, Annales de Physique, vol.26, issue.6, pp.1-167, 2001. ,
DOI : 10.1051/anphys:200106001
URL : https://hal.archives-ouvertes.fr/in2p3-00019832
Cross-correlations in NMR, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.37, issue.3, p.191, 2000. ,
DOI : 10.1016/S0079-6565(00)00023-6
Interference EEects in the Relaxaation of a Pair of Unlike Spin 1/2 Nuclei, Journal of Magnetic Resonance, vol.60, pp.437-452, 1984. ,
Accurate Sampling of High-Frequency Motions in Proteins by Steady-State 15 N-{ 1 H} Nuclear Overhauser EEect Measurements in the Presence of Cross-Correlated Relaxation, Journal of the American Chemical Society, issue.17, pp.1316048-6049 ,
On the measurement of 15N???{1H} nuclear Overhauser effects. 2. Effects of the saturation scheme and water signal suppression, Journal of Magnetic Resonance, vol.207, issue.2, pp.294-303 ,
DOI : 10.1016/j.jmr.2010.09.014
URL : https://hal.archives-ouvertes.fr/hal-00422173
Protein Dynamics from Nuclear Spin Relaxation, pp.2015-2022 ,
URL : https://hal.archives-ouvertes.fr/tel-01333232
Theory for nuclear magnetic relaxation of probes in anisotropic systems: application to cholesterol in phospholipid vesicles, Biochemistry, vol.20, issue.16, pp.4618-4628 ,
Fractional protein dynamics seen by nuclear magnetic resonance spectroscopy: Relating molecular dynamics simulation and experiment, The Journal of Chemical Physics, vol.93, issue.14, p.145101, 2010. ,
DOI : 10.1021/ja00168a070
URL : https://hal.archives-ouvertes.fr/hal-00593171
Toward the Characterization of Fractional Stochastic Processes Underlying Methyl Dynamics in Proteins, The Journal of Physical Chemistry B, vol.116, issue.43, pp.12955-12965 ,
DOI : 10.1021/jp307050v
The physical basis of model-free analysis of NMR relaxation data from proteins and complex uids, The Journal of Chemical Physics, issue.22, p.131224507, 2009. ,
NMR Order Parameters of Biomolecules: A New Analytical Representation and Application to the Gaussian Axial Fluctuation Model, Journal of the American Chemical Society, vol.116, issue.18, pp.8426-8427, 1994. ,
DOI : 10.1021/ja00097a084
Slow Motional ESR in Complex Fluids: The Slowly Relaxing Local Structure Model of Solvent Cage Effects, The Journal of Physical Chemistry, vol.99, issue.27, pp.10995-11006, 1995. ,
DOI : 10.1021/j100027a047
Dynamics of Unfolded Proteins:?? Incorporation of Distributions of Correlation Times in the Model Free Analysis of NMR Relaxation Data, Journal of the American Chemical Society, vol.121, issue.37, pp.8671-8672 ,
DOI : 10.1021/ja9910412
Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP, Journal of Biomolecular NMR, vol.44, issue.3, pp.163-177 ,
DOI : 10.1007/s10858-008-9280-0
Philippe Pelupessy, and Fabien Ferrage. Distribution of Pico-and Nanosecond Motions in Disordered Proteins from Nuclear Spin Relaxation, Biophysical Journal, vol.109, issue.5, pp.988-999 ,
Kinetic response of a photoperturbed allosteric protein, Proceedings of the National Academy of Sciences, pp.11725-11730 ,
DOI : 10.1002/jcc.20065
Conformer generation under restraints, Current Opinion in Structural Biology, vol.16, issue.2, pp.160-165 ,
Hidden alternative structures of proline isomerase essential for catalysis, Nature, vol.71, issue.7273, pp.669-673 ,
DOI : 10.1038/nature08615
Protein structural ensembles are revealed by redefining X-ray electron density noise, Proceedings of the National Academy of Sciences, vol.28, issue.1, pp.237-242 ,
DOI : 10.1093/nar/28.1.235
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3890839
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy, Journal of the American Chemical Society, vol.132, issue.45, pp.15957-15967 ,
DOI : 10.1021/ja100726a
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion, Angewandte Chemie International Edition, vol.120, issue.46, pp.11005-11009 ,
DOI : 10.1002/anie.201103944
Conformational Flexibility of a Microcrystalline Globular Protein: Order Parameters by Solid-State NMR Spectroscopy, Journal of the American Chemical Society, vol.128, issue.35, pp.11505-11512 ,
DOI : 10.1021/ja062443u
Conformational entropy in molecular recognition by proteins, Nature, vol.10, issue.7151, pp.325-329 ,
DOI : 10.1038/nature05959
NMR Residual Dipolar Couplings as Probes of Biomolecular Dynamics, Chemical Reviews, vol.106, issue.5, pp.1720-1736 ,
Protein Conformational Flexibility from Structure-Free Analysis of NMR Dipolar Couplings: Quantitative and Absolute Determination of Backbone Motion in Ubiquitin, Angewandte Chemie, vol.317, issue.23, pp.4218-4221 ,
DOI : 10.1002/ange.200900476
Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics, Journal of Biomolecular NMR, vol.23, issue.3, pp.41139-155 ,
DOI : 10.1007/s10858-008-9244-4
Accessing ns?????s side chain dynamics in ubiquitin with methyl RDCs, Journal of Biomolecular NMR, vol.122, issue.51???55, pp.23-44 ,
DOI : 10.1007/s10858-009-9354-7
De Novo Determination of Bond Orientations and Order Parameters from Residual Dipolar Couplings with High Accuracy, Journal of the American Chemical Society, vol.125, issue.34, pp.10164-10165, 2003. ,
DOI : 10.1021/ja035904+
Model-Free Analysis of Protein Backbone Motion from Residual Dipolar Couplings, Journal of the American Chemical Society, vol.124, issue.20, pp.5822-5833 ,
DOI : 10.1021/ja011883c
Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease, Biochemistry, vol.28, issue.23, pp.288972-8979, 1989. ,
DOI : 10.1021/bi00449a003
Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR Relaxation, Biochemistry, vol.33, issue.19, pp.335984-6003 ,
DOI : 10.1021/bi00185a040
Probing the Effect of Temperature on the Backbone Dynamics of the Human ??-Lactalbumin Molten Globule, Journal of the American Chemical Society, vol.130, issue.46, pp.15318-15326 ,
DOI : 10.1021/ja802967k
Fractional 13C enrichment of isolated carbons using [1-13C]- or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone C?? and side-chain methyl positions in proteins, Journal of Biomolecular NMR, vol.7, issue.3, pp.199-212 ,
DOI : 10.1007/s10858-007-9158-6
Chapter 1. Isotope-Labelling of Methyl Groups for NMR Studies of Large Proteins, RSC Biomolecular Sciences, pp.1-24, 2012. ,
Conformational stabilization of ubiquitin yields potent and selective inhibitors of USP7, Nature Chemical Biology, vol.20, issue.1, pp.51-58 ,
DOI : 10.1038/nchembio.1134
Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution, Science, vol.117, issue.7147, pp.3201471-1475 ,
DOI : 10.1038/nature05858
Dynamical characterization of residual and non-native structures in a partially folded protein by 15N NMR relaxation using a model based on a distribution of correlation times, Protein Science, vol.11, issue.4, pp.957-964 ,
DOI : 10.1110/ps.4000102
N NMR Relaxation in Proteins, Journal of the American Chemical Society, vol.123, issue.13, pp.3055-3063 ,
DOI : 10.1021/ja003803v
Nanosecond to Microsecond Protein Dynamics Probed by Magnetic Relaxation Dispersion of Buried Water Molecules, Journal of the American Chemical Society, vol.130, issue.5, pp.1774-1787 ,
DOI : 10.1021/ja0775873
Deuterium Spin Probes of Side-Chain Dynamics in Proteins. 1. Measurement of Five Relaxation Rates per Deuteron in 13C- Labeled and Fractionally 2H-Enriched Proteins in Solution, Journal of the American Chemical Society, issue.22, pp.1246439-6448 ,
Deuterium Spin Probes of Side-Chain Dynamics in Proteins. 2. Spectral Density Mapping and Identification of Nanosecond Time-Scale Side-Chain Motions, Journal of the American Chemical Society, vol.124, issue.22, pp.6449-6460 ,
DOI : 10.1021/ja012498q
Toward Quantitative Interpretation of Methyl Side-Chain Dynamics from NMR by Molecular Dynamics Simulations, Journal of the American Chemical Society, vol.129, issue.46, pp.14146-14147 ,
An improved refocused INEPT experiment. Application for sensitivity enhancement and spectral editing in 13C NMR, Journal of Magnetic Resonance, vol.77, issue.1, pp.170-174, 1969. ,
Studies of chemical exchange by nuclear magnetic relaxation in the rotating frame, Molecular Physics, vol.249, issue.4, pp.553-559 ,
DOI : 10.1021/ja00862a015
Rotating-Frame Relaxation with Weak Radio Frequency Fields, Journal of the American Chemical Society, vol.126, issue.7, pp.2247-2256 ,
DOI : 10.1021/ja038721w
Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead, Journal of Magnetic Resonance, vol.221, pp.1-4 ,
DOI : 10.1016/j.jmr.2012.05.005
On the measurement of 15N???{1H} nuclear Overhauser effects, Journal of Magnetic Resonance, vol.192, issue.2, pp.302-313 ,
DOI : 10.1016/j.jmr.2008.03.011
Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity, Journal of the American Chemical Society, vol.114, issue.26, pp.10663-10665 ,
DOI : 10.1021/ja00052a088
A new look at the statistical model identiication. Automatic Control, IEEE Transactions on, vol.19, issue.6, pp.716-723, 1974. ,
Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diiusion tensor, Journal of Biomolecular NMR, vol.40, issue.2, pp.121-133 ,
Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diiusion spaces, Journal of Biomolecular NMR, vol.40, issue.2, pp.107-119 ,
C NMR Relaxation Techniques for the Study of Protein Methyl Group Dynamics in Solution, Journal of the American Chemical Society, vol.121, issue.12, pp.2891-2902 ,
DOI : 10.1021/ja983758f
The ???long tail??? of the protein tumbling correlation function: observation by 1H NMR relaxometry in a wide frequency and concentration range, Journal of Biomolecular NMR, vol.75, issue.4, pp.403-415 ,
DOI : 10.1007/s10858-015-0001-1
AILM 2015 Patractical school, pp.2015-2016 ,
Zero--eld nuclear magnetic resonance. Physical review letters, p.501807, 1983. ,
Zero field NMR and NQR, The Journal of Chemical Physics, vol.5, issue.10, p.4877, 1985. ,
DOI : 10.1063/1.435038
Construction of a Liquid-State NMR DNP Shuttle Spectrometer: First Experimental Results and Evaluation of Optimal Performance Characteristics, Applied Magnetic Resonance, vol.106, issue.3-4, pp.3-4301 ,
DOI : 10.1007/s00723-008-0131-7
Increase in signal-to-noise ratio of> 10,000 times in liquid-state NMR, Proceedings of the National Academy of Sciences, vol.100, issue.18, pp.10158-10163, 2003. ,
Three--eld NMR to preserve hyperpolarized proton magnetization as long-lived states in moderate magnetic elds, Chemical Physics Letters, vol.512, pp.4-6151 ,
Field cycling by fast NMR probe transfer: Design and application in field-dependent CIDNP experiments, Applied Magnetic Resonance, vol.46, issue.2-3, pp.211-225 ,
DOI : 10.1007/BF03162162
Magnet Design with High B0 Homogeneity for Fast-Field-Cycling NMR Applications, Journal of Magnetic Resonance, vol.149, issue.1, pp.22-28 ,
DOI : 10.1006/jmre.2000.2279
NMR field-cycling spectroscopy: principles and a]lications, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.18, issue.3, pp.171-276 ,
DOI : 10.1016/0079-6565(86)80004-8
Proton Magnetic Shielding Tensor in Liquid Water, Journal of the American Chemical Society, vol.124, issue.40, pp.12031-12041 ,
DOI : 10.1021/ja026981s
Morphology of porous media studied by nuclear magnetic resonance, The Journal of Chemical Physics, vol.106, issue.18, p.7802, 1997. ,
DOI : 10.1016/0730-725X(91)90365-S
Nuclear magnetic relaxation of liquids in porous media, New Journal of Physics, vol.13, issue.3, pp.35016-2011 ,
DOI : 10.1088/1367-2630/13/3/035016
NMR studies of multiple relaxations in polymers, Journal of Polymer Science Part C: Polymer Symposia, vol.70, issue.1, pp.33-48 ,
DOI : 10.1002/polc.5070140107
NMR Relaxation, NMR Spectroscopy of Polymers, pp.169-197, 2004. ,
DOI : 10.1007/978-3-662-08982-8_7
Shuttle DNP spectrometer with a two-center magnet, Physical Chemistry Chemical Physics, vol.15, issue.3, p.125830, 2010. ,
DOI : 10.1039/c002814m
URL : http://hdl.handle.net/11858/00-001M-0000-0012-D69D-7
Shuttling device for high-resolution measurements of relaxation and related phenomena in solution at low field, using a shared commercial 500 MHz NMR instrument, Magnetic Resonance in Chemistry, vol.84, issue.10, pp.753-768 ,
DOI : 10.1002/mrc.1264
Soft Magnetic Materials and semi--nished Products. 2002-01. US Patent App, p.466932 ,
Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2??kDa microtubule associated protein 2c, Journal of Biomolecular NMR, vol.52, issue.4, pp.291-301 ,
DOI : 10.1007/s10858-013-9761-7
Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution, Progress in nuclear magnetic resonance spectroscopy, pp.93-158, 1999. ,
An eecient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-speciic resonance assignments of isotopically-enriched proteins, Journal of the American Chemical Society, vol.114, issue.27, pp.10974-10975 ,
Assignment of side-chain 13C resonances in perdeuterated proteins, Journal of the American Chemical Society, vol.117, issue.14, pp.4187-4188, 1995. ,
Iterative schemes for bilinear operators; application to spin decoupling, Journal of Magnetic Resonance (1969), vol.77, issue.2, pp.274-293, 1969. ,
DOI : 10.1016/0022-2364(88)90178-3
Broadband homonuclear cross polarization using ip--op spectroscopy, Journal of Magnetic Resonance, issue.2, pp.91437-443, 1969. ,
DOI : 10.1016/0022-2364(91)90210-k
The role of level anti-crossings in nuclear spin hyperpolarization, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.81, pp.1-36 ,
DOI : 10.1016/j.pnmrs.2014.06.001
High-resolution heteronuclear NMR spectroscopy in an inhomogeneous magnetic eld, Journal of Magnetic Resonance, vol.89, issue.2, pp.273-286, 1969. ,
Assignment of carbon-13 NMR spectra via double-quantum coherence, Journal of Magnetic Resonance (1969), vol.43, issue.3, pp.478-483, 1969. ,
DOI : 10.1016/0022-2364(81)90060-3
Investigation of complex networks of spin-spin coupling by twodimensional NMR, Journal of Magnetic Resonance, vol.44, issue.3, pp.542-561, 1969. ,
Polarization of Nuclei in Metals, Physical Review, vol.92, issue.2, pp.411-415 ,
DOI : 10.1103/PhysRev.92.411
Polarization of Nuclear Spins in Metals, Physical Review, vol.92, issue.1, pp.212-213 ,
DOI : 10.1103/PhysRev.92.212.2
An improved sequence for broadband decoupling: WALTZ-16, Journal of Magnetic Resonance (1969), vol.52, issue.2, pp.335-338, 1969. ,
DOI : 10.1016/0022-2364(83)90207-X
Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins, Biochemical and Biophysical Research Communications, vol.113, issue.3, pp.967-974 ,
DOI : 10.1016/0006-291X(83)91093-8
Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence, Journal of the American Chemical Society, vol.101, issue.16, pp.4481-4484, 1979. ,
DOI : 10.1021/ja00510a007
Selection of coherence-transfer pathways in NMR pulse experiments, Journal of Magnetic Resonance, vol.58, issue.3, pp.370-388, 1969. ,
URL : https://hal.archives-ouvertes.fr/hal-00730604
Application of Phase Sensitive Two-Dimensional Correlated Spectroscopy (COSY) for measurements of 1H-1H Spin-Spin Coupling Constants in Proteins, NMR in Structural Biology: A Collection of Papers by Kurt Wüthrich, p.114, 1995. ,
Computer-optimized decoupling scheme for wideband applications and low-level operation, Journal of Magnetic Resonance (1969), vol.64, issue.3, pp.547-552, 1969. ,
DOI : 10.1016/0022-2364(85)90122-2
C NMR Spectroscopy of Methyl Groups in Very High Molecular Weight Proteins and Protein Complexes, Journal of the American Chemical Society, vol.125, issue.34, pp.10420-10428 ,
DOI : 10.1021/ja030153x
Structural characterization of a highly???ordered ???molten globule??? at low pH, Nature Structural Biology, vol.31, issue.1, pp.23-29 ,
DOI : 10.1107/S0021889891004399
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin, Science, vol.262, issue.5135, pp.892-896 ,
A residue-specific NMR view of the non-cooperative unfolding of a molten globule, Natural Structural Biology, vol.29, issue.8, pp.630-634 ,
DOI : 10.1016/0022-2836(91)80073-4
Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins, Methods, vol.34, issue.1, pp.121-132 ,
DOI : 10.1016/j.ymeth.2004.03.009
Chemical exchange in NMR, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.43, issue.3-4, pp.63-103 ,
DOI : 10.1016/j.pnmrs.2003.08.001
1-Aryl-3,3-dialkyltriazenes as Tumor Inhibitors, The Journal of Organic Chemistry, vol.22, issue.2, pp.200-203 ,
An Adaptive Metropolis Algorithm, Bernoulli, vol.7, issue.2, pp.2001-2005 ,
DOI : 10.2307/3318737
URL : http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.48.8948
Simple method for the generation of multiple homogeneous field volumes inside the bore of superconducting magnets, Scientific Reports, vol.100, issue.1, pp.12200-2015 ,
DOI : 10.1073/pnas.1133497100
URL : https://hal.archives-ouvertes.fr/hal-01223310
Comparative study of the physicochemical properties of six clinical low molecular weight gadolinium contrast agents, Contrast Media & Molecular Imaging, vol.7, issue.3, pp.128-137 ,
DOI : 10.1002/cmmi.100
Towards MRI contrast agents of improved efficacy. NMR relaxometric investigations of the binding interaction to HSA of a novel heptadentate macrocyclic triphosphonate Gd(III)-complex, Journal of Biological Inorganic Chemistry, vol.2, issue.4, pp.470-479, 1997. ,
DOI : 10.1007/s007750050158
Sample Shuttling Relaxometry of Contrast Agents: NMRD Profiles above 1 T with a Single Device, Applied Magnetic Resonance, vol.293, issue.3, pp.237-246 ,
DOI : 10.1007/s00723-015-0751-7
URL : https://hal.archives-ouvertes.fr/hal-01266671
Identiication of compounds with binding aanity to proteins via magnetization transfer from bulk water, Journal of Biomolecular NMR, vol.18, issue.1, pp.65-68, 2000. ,
DOI : 10.1023/A:1008354229396
Field-Cycling NMR Applied to Macromolecular Structure and Dynamics, NMR as a Structural Tool for Macromolecules: Current Status and Future Directions, pp.123-132, 1996. ,
Global and Local Mobility of Apocalmodulin Monitored through Fast-Field Cycling Relaxometry, Biophysical Journal, vol.97, issue.6, pp.1765-1771 ,
DOI : 10.1016/j.bpj.2009.07.005
Seeking Higher Resolution and Sensitivity for NMR of Quadrupolar Nuclei at Ultrahigh Magnetic Fields, Journal of the American Chemical Society, vol.124, issue.20, pp.5634-5635 ,
DOI : 10.1021/ja025849p