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1. Full Text Probing transient conformational states of proteins by solid-state R 1ρ relaxation-dispersion NMR spectroscopy
by Ma, Peixiang and Haller, Jens D and Zajakala, Jérémy and Macek, Pavel and Sivertsen, Astrid C and Willbold, Dieter and Boisbouvier, Jérôme and Schanda, Paul
Angewandte Chemie - International Edition, ISSN 1433-7851, 04/2014, Volume 53, Issue 17, pp. 4312 - 4317
relaxation dispersion | transient conformations | solid-state NMR spectroscopy | ubiquitin | protein dynamics
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2. Full Text Probing Transient Conformational States of Proteins by Solid-State R11 Relaxation- Dispersion NMR Spectroscopy
by Ma, PX and Haller, JD and Zajakala, J and Macek, P and Sivertsen, AC and Willbold, D and Boisbouvier, J and Schanda, P
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, ISSN 1433-7851, 04/2014, Volume 53, Issue 17, pp. 4312 - 4317
The function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally... 
SLOW MOTIONS | relaxation dispersion | transient conformations | RESONANCE | solid-state NMR spectroscopy | protein dynamics | RESOLUTION | DYNAMICS | INTERMEDIATE | PERDEUTERATED PROTEINS | CHEMISTRY, MULTIDISCIPLINARY | ubiquitin
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3. Full Text NMR dispersion investigations of enzymatically degraded bovine articular cartilage
by Rössler, Erik and Mattea, Carlos and Stapf, Siegfried
Magnetic Resonance in Medicine, ISSN 0740-3194, 05/2015, Volume 73, Issue 5, pp. 2005 - 2014
Purpose Cross‐relaxation of protons with 14N nuclei in proteins enhances relaxivity in the quadrupolar dip range of typically 2–3 MHz Larmor frequency. The... 
soft matter | low field NMR | relaxometry | quadrupolar dips | cartilage | COLLAGEN | GLYCOSAMINOGLYCANS | CROSS-RELAXATION | HYDRATION | FIELD-CYCLING NMR | MICROSCOPIC MRI | SPIN-LATTICE-RELAXATION | SPECTROSCOPY | DYNAMICS | KNEE OSTEOARTHRITIS | RADIOLOGY, NUCLEAR MEDICINE & MEDICAL IMAGING | Body Water - metabolism | Collagen - metabolism | Nitrogen - metabolism | Animals | Trypsin - pharmacology | Cartilage, Articular - metabolism | Cattle | Glycosaminoglycans - metabolism | Collagenases - pharmacology | Osteoarthritis - metabolism | Proton Magnetic Resonance Spectroscopy - methods | Glycosaminoglycans | Nuclear magnetic resonance | Osteoarthritis | Collagen | Investigations
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4. Full Text Excited States of Nucleic Acids Probed by Proton Relaxation Dispersion NMR Spectroscopy
by Juen, Michael Andreas and Wunderlich, Christoph Hermann and Nußbaumer, Felix and Tollinger, Martin and Kontaxis, Georg and Konrat, Robert and Hansen, D. Flemming and Kreutz, Christoph
Angewandte Chemie International Edition, ISSN 1433-7851, 09/2016, Volume 55, Issue 39, pp. 12008 - 12012
In this work an improved stable isotope labeling protocol for nucleic acids is introduced. The novel building blocks eliminate/minimize homonuclear 13C and 1H... 
stable isotope labeling | RNA | NMR spectroscopy | DNA | proton relaxation dispersion | CTAR DNA | RECOGNITION | TIME | CHAPERONE | H-1 | CHEMISTRY, MULTIDISCIPLINARY | NUCLEOTIDES | H-1-NMR CHEMICAL-SHIFTS | RNA DYNAMICS | HIV-1 NUCLEOCAPSID PROTEIN | CONFORMATIONAL STATES | Nuclear magnetic resonance spectroscopy | Investigations | Labeling | Experiments | Deoxyribonucleic acid--DNA | Communications | Communication
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5. Full Text Resolving biomolecular motion and interactions by R2 and R1ρ relaxation dispersion NMR
by Walinda, Erik and Morimoto, Daichi and Sugase, Kenji
Methods, ISSN 1046-2023, 09/2018, Volume 148, pp. 28 - 38
Among the tools of structural biology, NMR spectroscopy is unique in that it not only derives a static three-dimensional structure, but also provides an... 
DNA/RNA dynamics | Biomolecular interactions | Chemical exchange | Relaxation dispersion | Conformational exchange | Protein dynamics | NMR spectroscopy
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6. Full Text Conformational Dynamics in the Core of Human Y145Stop Prion Protein Amyloid Probed by Relaxation Dispersion NMR
by Shannon, Matthew D and Theint, Theint and Mukhopadhyay, Dwaipayan and Surewicz, Krystyna and Surewicz, Witold K and Marion, Dominique and Schanda, Paul and Jaroniec, Christopher P
ChemPhysChem, ISSN 1439-4235, 01/2019, Volume 20, Issue 2, pp. 311 - 317
Microsecond to millisecond timescale backbone dynamics of the amyloid core residues in Y145Stop human prion protein (PrP) fibrils were investigated by using... 
Amyloids | prions | relaxation dispersion | NMR spectroscopy | protein dynamics | BACKBONE DYNAMICS | TIMESCALES | SOLID-STATE NMR | RESOLUTION | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | CHEMISTRY, PHYSICAL | PRINCIPLES | FIBRILS | SPECTROSCOPY | MAGNETIC-RESONANCE | ASSIGNMENT | COUPLINGS | Life Sciences | Biomolecules | Biochemistry, Molecular Biology
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7. Full Text Resolving biomolecular motion and interactions by R-2 and R-1 rho relaxation dispersion NMR
by Walinda, E and Morimoto, D and Sugase, K
METHODS, ISSN 1046-2023, 09/2018, Volume 148, pp. 28 - 38
Among the tools of structural biology, NMR spectroscopy is unique in that it not only derives a static three-dimensional structure, but also provides an... 
DNA/RNA dynamics | INVISIBLE EXCITED-STATES | Chemical exchange | Relaxation dispersion | ROTATING-FRAME RELAXATION | 3-DIMENSIONAL FOURIER SYNTHESIS | TRANSVERSE RELAXATION | Conformational exchange | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR-MAGNETIC-RESONANCE | BIOCHEMICAL RESEARCH METHODS | CHARACTERIZING CHEMICAL-EXCHANGE | Protein dynamics | MOLECULAR-WEIGHT PROTEINS | Biomolecular interactions | NMR spectroscopy | TIME-SCALE DYNAMICS | MULTIPLE-QUANTUM RELAXATION
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8. Full Text Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain H-1 Probes
by Hansen, AL and Lundstrom, P and Velyvis, A and Kay, LE and Institutionen för fysik, kemi och biologi and Molekylär Bioteknik and Linköpings universitet and Tekniska högskolan
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, ISSN 0002-7863, 02/2012, Volume 134, Issue 6, pp. 3178 - 3189
A Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for quantifying millisecond time-scale chemical exchange at side-chain H-1 positions... 
STRUCTURE GENERATION | INVISIBLE EXCITED-STATES | ACCURATE MEASUREMENT | IMPROVED SENSITIVITY | CHEMICAL-SHIFTS | TRANSVERSE RELAXATION | METHYL-GROUPS | DIPOLAR COUPLINGS | ATOMIC-RESOLUTION | CHEMISTRY, MULTIDISCIPLINARY | TIME-SCALE DYNAMICS | Teknik och teknologier | TEKNIKVETENSKAP | Engineering and Technology | TECHNOLOGY
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9. Cross Validation of the Structure of a Transiently Formed and Low Populated FF Domain Folding Intermediate Determined by Relaxation Dispersion NMR and CS-Rosetta
by Barette, Julia Audrey
11/2011
The atomic resolution structure of a low populated and transiently formed on-pathway folding intermediate of the FF domain from human HYPA/FBP11 has recently... 
Folding Intermediate | Nuclear Magnetic Resonance (NMR) Spectroscopy | 0487 | FF domain | CPMG Relaxation Dispersion NMR | Protein Structure | Protein Folding
Dissertation
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10. Full Text Increasing the exchange time-scale that can be probed by CPMG relaxation dispersion NMR
by Vallurupalli, Pramodh and Bouvignies, Guillaume and Kay, Lewis E
Journal of Physical Chemistry B, ISSN 1520-6106, 12/2011, Volume 115, Issue 49, pp. 14891 - 14900
Carr-Purcell-Meiboom-Gill relaxation dispersion NMR spectroscopy has emerged as a valuable tool to characterize conformational exchange between major and minor... 
FOLDING INTERMEDIATE | BIOLOGICAL MACROMOLECULES | PROTEIN-STRUCTURE GENERATION | NUCLEAR-MAGNETIC-RESONANCE | CHEMISTRY, PHYSICAL | CHEMICAL-EXCHANGE | CAVITY MUTANT | T4 LYSOZYME | R-1-RHO RELAXATION | EXCITED-STATES | SH3 DOMAIN | Time Factors | Muramidase - chemistry | Muramidase - genetics | Amides - chemistry | Nuclear Magnetic Resonance, Biomolecular | Nitrogen Isotopes - chemistry | Proteins - chemistry | Amino Acid Substitution | Usage | Amides | Biomolecules | Nuclear magnetic resonance spectroscopy | Research | Structure | Electric properties | Excited state chemistry | Exchange | Data sets | Tools | Dispersions | Excitation | Nuclear magnetic resonance | Inclusions
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11. Full Text The Energetics of a Three‐State Protein Folding System Probed by High‐Pressure Relaxation Dispersion NMR Spectroscopy
by Tugarinov, Vitali and Libich, David S and Meyer, Virginia and Roche, Julien and Clore, G. Marius
Angewandte Chemie International Edition, ISSN 1433-7851, 09/2015, Volume 54, Issue 38, pp. 11157 - 11161
The energetic and volumetric properties of a three‐state protein folding system, comprising a metastable triple mutant of the Fyn SH3 domain, have been... 
high‐pressure NMR spectroscopy | protein folding | relaxation dispersion | kinetics | proteins | high-pressure NMR spectroscopy | DEPENDENT NMR | CAVITIES | STABILITY | PERTURBATION | COMPRESSIBILITY | DENATURATION | CHEMISTRY, MULTIDISCIPLINARY | PATHWAY | DYNAMICS | INTERMEDIATE | EXCHANGE | Proteins - chemistry | Nuclear Magnetic Resonance, Biomolecular - methods | Pressure | Protein Folding | Proteins | Pictures | Compressibility | Pathways | Molar volume | Dispersions | Nuclear magnetic resonance | NMR spectroscopy | Folding
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12. Full Text Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy
by Lundström, Patrik and Hansen, D. Flemming and Vallurupalli, Pramodh and Kay, Lewis E
Journal of the American Chemical Society, ISSN 0002-7863, 02/2009, Volume 131, Issue 5, pp. 1915 - 1926
Carr-Purcell-Meiboom-Gill relaxation dispersion NMR spectroscopy can provide detailed information about low populated, invisible states of protein molecules,... 
SEQUENCE HOMOLOGY | SPIN RELAXATION | C-13 | NUCLEAR-MAGNETIC-RESONANCE | C-ALPHA | DYNAMICS | DIPOLAR COUPLINGS | SECONDARY STRUCTURE | ADIABATIC PULSES | CHEMISTRY, MULTIDISCIPLINARY | SH3 DOMAIN | Deuterium | Protons | Amino Acid Sequence | Microfilament Proteins - chemistry | Nuclear Magnetic Resonance, Biomolecular - methods | Glucose - chemistry | Molecular Sequence Data | Saccharomyces cerevisiae Proteins - chemistry | src Homology Domains | Proteins | Nuclear magnetic resonance spectroscopy | Usage | Structure | Analysis | Excited state chemistry | Biological Sciences | Chemistry | Naturvetenskap | Kemi | Structural Biology | Biologiska vetenskaper | Strukturbiologi | Biokemi | Biochemistry | Natural Sciences | NUCLEAR-MAGNETIC-RESONANCE; SH3 DOMAIN; SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; DIPOLAR COUPLINGS; ADIABATIC PULSES; SPIN RELAXATION; C-ALPHA; DYNAMICS; C-13
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13. Full Text Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
by Hansen, D Flemming and Vallurupalli, Pramodh and Kay, Lewis E
Journal of Biomolecular NMR, ISSN 0925-2738, 7/2008, Volume 41, Issue 3, pp. 113 - 120
Currently the main focus of structural biology is the determination of static three-dimensional representations of biomolecules that for the most part... 
Biochemistry, general | Polymer Sciences | Biophysics/Biomedical Physics | Physics | BACKBONE DYNAMICS | SPIN RELAXATION | PROTON RELAXATION | SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR-MAGNETIC-RESONANCE | CHARACTERIZING CHEMICAL-EXCHANGE | SLOW DYNAMICS | DIPOLAR COUPLINGS | PANCREATIC TRYPSIN-INHIBITOR | MOTIONS | SH3 DOMAIN | Models, Molecular | Thermodynamics | Protein Conformation | Magnetic Resonance Spectroscopy - methods | Proteins - chemistry | Anisotropy | Nuclear magnetic resonance spectroscopy | Nuclear magnetic resonance--NMR
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14. Full Text Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy
by Hansen, D Flemming and Lundström, Patrik and Vallurupalli, Pramodh and Kay, Lewis E and Institutionen för fysik, kemi och biologi and Molekylär Bioteknik and Linköpings universitet and Tekniska högskolan
Nature Protocols, ISSN 1754-2189, 10/2009, Volume 4, Issue 11, pp. 1641 - 1648
The utility of nuclear magnetic resonance (NMR) spectroscopy as a tool for the study of biomolecular structure and dynamics has benefited from the development... 
BACKBONE DYNAMICS | CATALYSIS | C-13 | ACCURATE MEASUREMENT | TRANSVERSE RELAXATION | C-ALPHA | SEQUENCE | BIOCHEMICAL RESEARCH METHODS | MOTIONS | CHEMICAL-SHIFT DATA | SH3 DOMAIN | Deuterium | Protein Structure, Tertiary | Microfilament Proteins - chemistry | Isotope Labeling - methods | Chemical Fractionation | Nuclear Magnetic Resonance, Biomolecular - methods | Carbon Isotopes | Nitrogen Isotopes | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Usage | Nuclear magnetic resonance spectroscopy | Research | Affinity labeling | Methods | Conformation | Naturvetenskap | Natural Sciences
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15. Full Text A minor conformation of a lanthanide tag on adenylate kinase characterized by paramagnetic relaxation dispersion NMR spectroscopy
by Hass, Mathias A. S and Liu, Wei-Min and Agafonov, Roman V and Otten, Renee and Phung, Lien A and Schilder, Jesika T and Kern, Dorothee and Ubbink, Marcellus
Journal of Biomolecular NMR, ISSN 0925-2738, 2/2015, Volume 61, Issue 2, pp. 123 - 136
NMR relaxation dispersion techniques provide a powerful method to study protein dynamics by characterizing lowly populated conformations that are in dynamic... 
Biochemistry, general | Spectroscopy/Spectrometry | Relaxation dispersion | Adenylate kinase | Caged lanthanide NMR probe | Biophysics and Biological Physics | Protein dynamics | Lanthanide binding tags | Paramagnetic NMR | Physics | DOMAIN | BIOLOGICAL MACROMOLECULES | CHEMICAL-SHIFTS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MODEL | MOTIONS | SPECTROSCOPY | PSEUDOCONTACT SHIFTS | DYNAMICS | EXCHANGE | PROBE | EXCITED PROTEIN STATES | Adenylate Kinase - analysis | Models, Molecular | Protein Conformation | Lanthanoid Series Elements - chemistry | Adenylate Kinase - chemistry | Nuclear Magnetic Resonance, Biomolecular - methods | Rare earth metals | Enzymes | Nuclear magnetic resonance spectroscopy | Catalysis | Analysis | Protein binding
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16. Overview of Relaxation Dispersion NMR Spectroscopy to Study Protein Dynamics and Protein-Ligand Interactions
by Walinda, Erik and Morimoto, Daichi and Sugase, Kenji
Current protocols in protein science, 04/2018, Volume 92, Issue 1, p. e57
Proteins and nucleic acids are central to all biological processes. NMR spectroscopy has proven to be excellent for studying the dynamics of these... 
biomolecular interactions | relaxation dispersion | NMR spectroscopy | protein dynamics | chemical exchange
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17. Full Text Probing Microsecond Time Scale Dynamics in Proteins by Methyl H-1 Carr-Purcell-Meiboom-Gill Relaxation Dispersion NMR Measurements. Application to Activation of the Signaling Protein NtrC(r)
by Otten, Renee and Villali, Janice and Kern, Dorothee and