Protein Science, ISSN 0961-8368, 07/2012, Volume 21, Issue 7, pp. 996 - 1005
To examine the relationship between protein structural dynamics and measurable hydrogen exchange (HX) data, the detailed exchange behavior of most of the...
static and dynamic | protein folding | hydrogen exchange | protein dynamics | Staphylococcal nuclease | Hydrogen exchange | Protein dynamics | Protein folding | Static and dynamic | PROTON-EXCHANGE | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | STATE | PEPTIDE | CYTOCHROME-C | RATES | PATHWAY | FLUCTUATIONS | EQUILIBRIUM | Staphylococcus - enzymology | Hydrogen Bonding | Protein Structure, Secondary | Water - chemistry | Nuclear Magnetic Resonance, Biomolecular | Hydrogen - chemistry | Staphylococcus - chemistry | Micrococcal Nuclease - chemistry | Molecular Dynamics Simulation | Protein Folding | Solvents | Crystal structure
static and dynamic | protein folding | hydrogen exchange | protein dynamics | Staphylococcal nuclease | Hydrogen exchange | Protein dynamics | Protein folding | Static and dynamic | PROTON-EXCHANGE | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | STATE | PEPTIDE | CYTOCHROME-C | RATES | PATHWAY | FLUCTUATIONS | EQUILIBRIUM | Staphylococcus - enzymology | Hydrogen Bonding | Protein Structure, Secondary | Water - chemistry | Nuclear Magnetic Resonance, Biomolecular | Hydrogen - chemistry | Staphylococcus - chemistry | Micrococcal Nuclease - chemistry | Molecular Dynamics Simulation | Protein Folding | Solvents | Crystal structure
Journal Article
Protein Science, ISSN 0961-8368, 07/2012, Volume 21, Issue 7, pp. 987 - 995
To investigate the determinants of protein hydrogen exchange (HX), HX rates of most of the backbone amide hydrogens of Staphylococcal nuclease were measured by...
static and dynamic | hydrogen exchange | electrostatics | Staphylococcal nuclease | protein folding | cleanex‐PM | EX1 | Protein folding | Cleanex-PM | Hydrogen exchange | Electrostatics | Static and dynamic | PEPTIDE GROUP | ENSEMBLE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTECTION FACTORS | STATE | PREDICTION | ORIGIN | FOLDING PATHWAY | FLUCTUATIONS | DYNAMICS | cleanex-PM | Staphylococcus - enzymology | Models, Chemical | Nuclear Magnetic Resonance, Biomolecular | Static Electricity | Hydrogen - chemistry | Staphylococcus - chemistry | Micrococcal Nuclease - chemistry | Protein Folding
static and dynamic | hydrogen exchange | electrostatics | Staphylococcal nuclease | protein folding | cleanex‐PM | EX1 | Protein folding | Cleanex-PM | Hydrogen exchange | Electrostatics | Static and dynamic | PEPTIDE GROUP | ENSEMBLE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTECTION FACTORS | STATE | PREDICTION | ORIGIN | FOLDING PATHWAY | FLUCTUATIONS | DYNAMICS | cleanex-PM | Staphylococcus - enzymology | Models, Chemical | Nuclear Magnetic Resonance, Biomolecular | Static Electricity | Hydrogen - chemistry | Staphylococcus - chemistry | Micrococcal Nuclease - chemistry | Protein Folding
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2014, Volume 111, Issue 45, pp. 15975 - 15980
Long-time molecular dynamics (MD) simulations are now able to fold small proteins reversibly to their native structures [Lindorff-Larsen K, Piana S, Dror RO,...
Protons | Hydrogen | Protein folding | Ubiquitins | Force field | Molecular dynamics | Amides | Trajectories | Kinetics | Free energy | HX | Denatured states | Unfolded state | DENATURANT | MULTIDISCIPLINARY SCIENCES | denatured states | BOND FORMATION | FRET SPECTROSCOPY | molecular dynamics | FAST-FOLDING PROTEINS | EXCITED-STATES | UNFOLDED-STATE | unfolded state | RIBONUCLEASE-A | MODELS | LAMBDA-REPRESSOR | protein folding | MOLECULAR-DYNAMICS SIMULATIONS | Protein Structure, Tertiary | Deuterium Exchange Measurement | GTP-Binding Proteins - chemistry | Hydrogen Bonding | Protein Unfolding | Recombinant Proteins - chemistry | Hydrogen - chemistry | Physiological aspects | Protein research | Research | G proteins | ATOMIC AND MOLECULAR PHYSICS | Biological Sciences
Protons | Hydrogen | Protein folding | Ubiquitins | Force field | Molecular dynamics | Amides | Trajectories | Kinetics | Free energy | HX | Denatured states | Unfolded state | DENATURANT | MULTIDISCIPLINARY SCIENCES | denatured states | BOND FORMATION | FRET SPECTROSCOPY | molecular dynamics | FAST-FOLDING PROTEINS | EXCITED-STATES | UNFOLDED-STATE | unfolded state | RIBONUCLEASE-A | MODELS | LAMBDA-REPRESSOR | protein folding | MOLECULAR-DYNAMICS SIMULATIONS | Protein Structure, Tertiary | Deuterium Exchange Measurement | GTP-Binding Proteins - chemistry | Hydrogen Bonding | Protein Unfolding | Recombinant Proteins - chemistry | Hydrogen - chemistry | Physiological aspects | Protein research | Research | G proteins | ATOMIC AND MOLECULAR PHYSICS | Biological Sciences
Journal Article
Methods, ISSN 1046-2023, 2004, Volume 34, Issue 1, pp. 51 - 64
The measurement of amino acid-resolved hydrogen exchange (HX) has provided the most detailed information so far available on the structure and properties of...
Cytochrome c | Foldon | Theory | Protein folding | Protein function | Native state hydrogen exchange | Hydrogen exchange | Pulse labeling | EX1 | hydrogen exchange | MECHANISM | LANDSCAPE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | native state hydrogen exchange | protein function | pulse labeling | PROTONS | cytochrorne c | CYTOCHROME-C | NMR | RIBONUCLEASE-A | PATHWAY | KINETICS | DYNAMICS | INTERMEDIATE | protein folding | foldon | theory | Deuterium Exchange Measurement | Animals | Protein Structure, Secondary | Time Factors | Nuclear Magnetic Resonance, Biomolecular | Cytochrome c Group - chemistry | Hydrogen - chemistry | Protein Folding | Hydrogen-Ion Concentration
Cytochrome c | Foldon | Theory | Protein folding | Protein function | Native state hydrogen exchange | Hydrogen exchange | Pulse labeling | EX1 | hydrogen exchange | MECHANISM | LANDSCAPE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | native state hydrogen exchange | protein function | pulse labeling | PROTONS | cytochrorne c | CYTOCHROME-C | NMR | RIBONUCLEASE-A | PATHWAY | KINETICS | DYNAMICS | INTERMEDIATE | protein folding | foldon | theory | Deuterium Exchange Measurement | Animals | Protein Structure, Secondary | Time Factors | Nuclear Magnetic Resonance, Biomolecular | Cytochrome c Group - chemistry | Hydrogen - chemistry | Protein Folding | Hydrogen-Ion Concentration
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2013, Volume 110, Issue 19, pp. 7684 - 7689
The kinetic folding of ribonuclease H was studied by hydrogen exchange (HX) pulse labeling with analysis by an advanced fragment separation mass spectrometry...
Proteins | Molecules | Structural members | Protein folding | Hydrogen | Amides | Amino acids | Mass spectroscopy | Biochemistry | Kinetics | MOLTEN GLOBULE | OPTIONAL ERRORS | COLI RIBONUCLEASE-H | RESIDUAL STRUCTURE | MULTIDISCIPLINARY SCIENCES | UNFOLDED PROTEINS | INTERMEDIATE STATE | ATOMIC-RESOLUTION | ENERGY LANDSCAPE | NATIVE-STATE | RELAXATION DISPERSION | Escherichia coli - enzymology | Peptides - chemistry | Protein Denaturation | Ribonuclease H - chemistry | Amino Acids - chemistry | Software | Biophysics - methods | Hydrogen - chemistry | Mass Spectrometry - methods | Protein Folding | Hydrogen-Ion Concentration | Physiological aspects | Research | Health aspects | Mass spectrometry | Methods | Biological Sciences
Proteins | Molecules | Structural members | Protein folding | Hydrogen | Amides | Amino acids | Mass spectroscopy | Biochemistry | Kinetics | MOLTEN GLOBULE | OPTIONAL ERRORS | COLI RIBONUCLEASE-H | RESIDUAL STRUCTURE | MULTIDISCIPLINARY SCIENCES | UNFOLDED PROTEINS | INTERMEDIATE STATE | ATOMIC-RESOLUTION | ENERGY LANDSCAPE | NATIVE-STATE | RELAXATION DISPERSION | Escherichia coli - enzymology | Peptides - chemistry | Protein Denaturation | Ribonuclease H - chemistry | Amino Acids - chemistry | Software | Biophysics - methods | Hydrogen - chemistry | Mass Spectrometry - methods | Protein Folding | Hydrogen-Ion Concentration | Physiological aspects | Research | Health aspects | Mass spectrometry | Methods | Biological Sciences
Journal Article
The Journal of Chemical Physics, ISSN 0021-9606, 08/2017, Volume 147, Issue 7, p. 074302
Quantum reactive scattering calculations are reported for the ultracold hydrogen-exchange reaction and its non-reactive atom-exchange isotopic counterparts,...
CHEMISTRY | DYNAMICS | CHEMISTRY, PHYSICAL | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | MOLECULES | Exchanging | Organic chemistry | Equivalence | Chemical reactions | Rotational states | Wave functions | Nuclear reactions | Symmetry | Physics - Chemical Physics | INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY | Berry phase | molecular collisions | Atomic and Nuclear Physics | Inorganic and Physical Chemistry | geometric phase | ultracold chemistry
CHEMISTRY | DYNAMICS | CHEMISTRY, PHYSICAL | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | MOLECULES | Exchanging | Organic chemistry | Equivalence | Chemical reactions | Rotational states | Wave functions | Nuclear reactions | Symmetry | Physics - Chemical Physics | INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY | Berry phase | molecular collisions | Atomic and Nuclear Physics | Inorganic and Physical Chemistry | geometric phase | ultracold chemistry
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2014, Volume 111, Issue 24, pp. 8820 - 8825
Hydrogen exchange rates have become a valuable probe for studying the relationship between dynamics and structure and for dissecting the mechanism by which...
Proteins | Protons | Exchange rates | Chemical equilibrium | Solvents | Magnetization | Hydrogen | Protein folding | Amides | Nuclear magnetic resonance | Conformationally excited protein states | Amide exchange with solvent | CATALYSIS | ENERGY | BIOLOGICAL MACROMOLECULES | conformationally excited protein states | NMR-SPECTROSCOPY | MULTIDISCIPLINARY SCIENCES | NUCLEAR-MAGNETIC-RESONANCE | ATOMIC-RESOLUTION | SIDE-CHAINS | DYNAMICS | amide exchange with solvent | INTERMEDIATE | protein folding | CPMG RELAXATION DISPERSION | Protein Structure, Tertiary | Solvents - chemistry | Models, Molecular | Hydrogen - chemistry | Protein Folding | src Homology Domains | Animals | Nitrogen - chemistry | Chickens | Protein Denaturation | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Proto-Oncogene Proteins c-fyn - chemistry | Software | Kinetics | Proteins - chemistry | Hydrogen-Ion Concentration | Spectra | Analysis | Life Sciences | Biological Sciences
Proteins | Protons | Exchange rates | Chemical equilibrium | Solvents | Magnetization | Hydrogen | Protein folding | Amides | Nuclear magnetic resonance | Conformationally excited protein states | Amide exchange with solvent | CATALYSIS | ENERGY | BIOLOGICAL MACROMOLECULES | conformationally excited protein states | NMR-SPECTROSCOPY | MULTIDISCIPLINARY SCIENCES | NUCLEAR-MAGNETIC-RESONANCE | ATOMIC-RESOLUTION | SIDE-CHAINS | DYNAMICS | amide exchange with solvent | INTERMEDIATE | protein folding | CPMG RELAXATION DISPERSION | Protein Structure, Tertiary | Solvents - chemistry | Models, Molecular | Hydrogen - chemistry | Protein Folding | src Homology Domains | Animals | Nitrogen - chemistry | Chickens | Protein Denaturation | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Proto-Oncogene Proteins c-fyn - chemistry | Software | Kinetics | Proteins - chemistry | Hydrogen-Ion Concentration | Spectra | Analysis | Life Sciences | Biological Sciences
Journal Article
Journal of Physics B: Atomic, Molecular and Optical Physics, ISSN 0953-4075, 09/2016, Volume 49, Issue 19, p. 194004
The role of the geometric phase effect on chemical reaction dynamics is explored by examining the hydrogen exchange process in the fundamental H+HD reaction....
geometric phase effect | ultracold chemistry | molecular collisions | quantum reaction dynamics | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | CONICAL INTERSECTION | SCATTERING CALCULATIONS | COOLED COPPER TRIMER | SIMPLEST CHEMICAL-REACTION | MOLECULAR-SYSTEMS | POTENTIAL-ENERGY SURFACE | DIFFERENTIAL CROSS-SECTIONS | OPTICS | H+H-2 REACTION | COLLISION ENERGIES | STATE TRANSITION-PROBABILITIES | ATOMIC AND MOLECULAR PHYSICS | Inorganic and Physical Chemistry | CLASSICAL AND QUANTUM MECHANICS, GENERAL PHYSICS | Astronomy and Astrophysics
geometric phase effect | ultracold chemistry | molecular collisions | quantum reaction dynamics | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | CONICAL INTERSECTION | SCATTERING CALCULATIONS | COOLED COPPER TRIMER | SIMPLEST CHEMICAL-REACTION | MOLECULAR-SYSTEMS | POTENTIAL-ENERGY SURFACE | DIFFERENTIAL CROSS-SECTIONS | OPTICS | H+H-2 REACTION | COLLISION ENERGIES | STATE TRANSITION-PROBABILITIES | ATOMIC AND MOLECULAR PHYSICS | Inorganic and Physical Chemistry | CLASSICAL AND QUANTUM MECHANICS, GENERAL PHYSICS | Astronomy and Astrophysics
Journal Article
Protein Science, ISSN 0961-8368, 01/2003, Volume 12, Issue 1, pp. 153 - 160
Experiments were done to study the dynamic structural motions that determine protein hydrogen exchange (HX) behavior. The replacement of a solvent‐exposed...
Cytochrome c | hydrogen exchange | glycine mutations | pWT, pseudowild type | GdmCl, guanidinium chloride | HX, hydrogen exchange | local fluctuation | Cyt c, cytochrome c | Hydrogen exchange | Local fluctuation | Glycine mutations | AMIDE PROTON-EXCHANGE | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | LYSOZYME | STATE | CONFORMATION | NUCLEIC-ACIDS | CYTOCHROME-C | RATES | DYNAMICS | PANCREATIC TRYPSIN-INHIBITOR | cytochrome c
Cytochrome c | hydrogen exchange | glycine mutations | pWT, pseudowild type | GdmCl, guanidinium chloride | HX, hydrogen exchange | local fluctuation | Cyt c, cytochrome c | Hydrogen exchange | Local fluctuation | Glycine mutations | AMIDE PROTON-EXCHANGE | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | LYSOZYME | STATE | CONFORMATION | NUCLEIC-ACIDS | CYTOCHROME-C | RATES | DYNAMICS | PANCREATIC TRYPSIN-INHIBITOR | cytochrome c
Journal Article
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Full Text
Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy
Journal of the American Chemical Society, ISSN 0002-7863, 08/2017, Volume 139, Issue 32, pp. 11036 - 11039
A method is introduced that permits direct observation of the rates at which backbone amide hydrogens become protected from solvent exchange after rapidly...
BETA-HAIRPIN | RIBONUCLEASE-A | MECHANISM | PATHWAY | UBIQUITIN | DYNAMICS | STATE | DENATURATION | STAPHYLOCOCCAL NUCLEASE | CHEMISTRY, MULTIDISCIPLINARY | INSIGHTS | Ubiquitin | Nuclear magnetic resonance spectroscopy | Usage | Research | Isostatic pressing
BETA-HAIRPIN | RIBONUCLEASE-A | MECHANISM | PATHWAY | UBIQUITIN | DYNAMICS | STATE | DENATURATION | STAPHYLOCOCCAL NUCLEASE | CHEMISTRY, MULTIDISCIPLINARY | INSIGHTS | Ubiquitin | Nuclear magnetic resonance spectroscopy | Usage | Research | Isostatic pressing
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2013, Volume 110, Issue 50, pp. 20087 - 20092
Characterization of structure and dynamics of nonnative protein states is important for understanding molecular mechanisms of processes as diverse as folding,...
Proteins | Deuterium | Aggregation | Hydrogen | Ubiquitins | Ions | Mass spectroscopy | Amides | Biochemistry | Alcohols | Nonnative state | Protein dynamics | Conformational dynamics | Protein conformation | NMR-SPECTROSCOPY | MULTIDISCIPLINARY SCIENCES | protein dynamics | protein conformation | HYDROGEN/DEUTERIUM EXCHANGE | ESI-MS | IONS | HUMAN UBIQUITIN | nonnative state | A-STATE | conformational dynamics | ELECTRON-CAPTURE DISSOCIATION | ENERGY LANDSCAPE PERSPECTIVE | GAS-PHASE | DYNAMICS | Magnetic Resonance Spectroscopy | Ubiquitin - chemistry | Protein Conformation | Proteins - chemistry | Tandem Mass Spectrometry - methods | Deuterium Exchange Measurement - methods | Hydrogen-Ion Concentration | Research | Properties | Mass spectrometry | Methods | Protein-protein interactions | Biological Sciences
Proteins | Deuterium | Aggregation | Hydrogen | Ubiquitins | Ions | Mass spectroscopy | Amides | Biochemistry | Alcohols | Nonnative state | Protein dynamics | Conformational dynamics | Protein conformation | NMR-SPECTROSCOPY | MULTIDISCIPLINARY SCIENCES | protein dynamics | protein conformation | HYDROGEN/DEUTERIUM EXCHANGE | ESI-MS | IONS | HUMAN UBIQUITIN | nonnative state | A-STATE | conformational dynamics | ELECTRON-CAPTURE DISSOCIATION | ENERGY LANDSCAPE PERSPECTIVE | GAS-PHASE | DYNAMICS | Magnetic Resonance Spectroscopy | Ubiquitin - chemistry | Protein Conformation | Proteins - chemistry | Tandem Mass Spectrometry - methods | Deuterium Exchange Measurement - methods | Hydrogen-Ion Concentration | Research | Properties | Mass spectrometry | Methods | Protein-protein interactions | Biological Sciences
Journal Article
International Journal of Molecular Sciences, ISSN 1661-6596, 11/2018, Volume 19, Issue 11, p. 3406
Both experimental and computational methods are available to gather information about a protein's conformational space and interpret changes in protein...
Hydrogen exchange | Protein conformational sampling | Nuclear magnetic resonance | Mass spectrometry | Protein structure | ENSEMBLE | protein conformational sampling | hydrogen exchange | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | nuclear magnetic resonance | CHEMISTRY, MULTIDISCIPLINARY | COMPLEMENT COMPONENT C3 | INTERLEUKIN-8 | protein structure | NMR | FLUCTUATIONS | DYNAMICS | mass spectrometry | NATIVE-STATE | Models, Molecular | Protein Conformation | Deuterium Exchange Measurement | Humans | Interleukin-8 - chemistry | Complement C3b - chemistry
Hydrogen exchange | Protein conformational sampling | Nuclear magnetic resonance | Mass spectrometry | Protein structure | ENSEMBLE | protein conformational sampling | hydrogen exchange | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | nuclear magnetic resonance | CHEMISTRY, MULTIDISCIPLINARY | COMPLEMENT COMPONENT C3 | INTERLEUKIN-8 | protein structure | NMR | FLUCTUATIONS | DYNAMICS | mass spectrometry | NATIVE-STATE | Models, Molecular | Protein Conformation | Deuterium Exchange Measurement | Humans | Interleukin-8 - chemistry | Complement C3b - chemistry
Journal Article
PRS, ISSN 0961-8368, 8/1999, Volume 8, Issue 8, pp. 1571 - 1590
A database of hydrogen‐deuterium exchange results has been compiled for proteins for which there are published rates of out‐exchange in the native state,...
NMR | protein folding | hydrogen exchange | slow exchange core | COLI RIBONUCLEASE HI | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSITION-STATE | SRC SH3 DOMAIN | DENATURED STATE | BETA-SHEET PROTEIN | PARTIALLY FOLDED STATE | MOLTEN GLOBULE INTERMEDIATE | PANCREATIC TRYPSIN-INHIBITOR | EGG-WHITE LYSOZYME | MOLECULAR-DYNAMICS SIMULATIONS | Deuterium - chemistry | Animals | Protein Structure, Secondary | Cattle | Hydrogen - chemistry | Protein Folding | Hydrogen exchange | Slow exchange core | Protein folding
NMR | protein folding | hydrogen exchange | slow exchange core | COLI RIBONUCLEASE HI | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSITION-STATE | SRC SH3 DOMAIN | DENATURED STATE | BETA-SHEET PROTEIN | PARTIALLY FOLDED STATE | MOLTEN GLOBULE INTERMEDIATE | PANCREATIC TRYPSIN-INHIBITOR | EGG-WHITE LYSOZYME | MOLECULAR-DYNAMICS SIMULATIONS | Deuterium - chemistry | Animals | Protein Structure, Secondary | Cattle | Hydrogen - chemistry | Protein Folding | Hydrogen exchange | Slow exchange core | Protein folding
Journal Article