J. > MAGNETIC Sequence

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1\HIV\-1 \Vpu\ protein antagonizes innate restriction factor \BST\-2 via lipid-embedded helix-helix interactions
M. Skasko, Y. Wang, Y. Tian, A. Tokarev, J. Munguia, A. Ruiz, E. Stephens, S. Opella, and J. Guatelli. J. Biol. Chem., 287 (1): 58--67 (January 2012)
8 years ago by @nmrresource
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Acid
Hydrophilic
bilayers,Micelles,Models,Molecular,Molecular
Immunodeficiency
Sequence,Antigens,Biomolecular,CD,Cell
Regulatory
Sequence
Proteins,Humans,Hydrophobic
Proteins
Accessory
Cells,Human
Structure,Secondary,Tertiary,Thermodynamics,Viral
Data,Nuclear
Virus
Magnetic
and
Interactions,Immunity,Innate,Lipid
Amino
Proteins,HIV-1,HeLa
Binding,Protein
Membrane,GPI-Linked
Resonance,Protein
AcidHydrophilicbilayers,Micelles,Models,Molecular,MolecularImmunodeficiencySequence,Antigens,Biomolecular,CD,CellRegulatorySequenceProteins,Humans,HydrophobicProteinsAccessoryCells,HumanStructure,Secondary,Tertiary,Thermodynamics,ViralData,NuclearVirusMagneticandInteractions,Immunity,Innate,LipidAminoProteins,HIV-1,HeLaBinding,ProteinMembrane,GPI-LinkedResonance,Protein
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1\NMR\ structure determination of a membrane protein with two transmembrane helices in micelles: \MerF\ of the bacterial mercury detoxification system
S. Howell, M. Mesleh, and S. Opella. Biochemistry, 44 (13): 5196--5206 (April 2005)
8 years ago by @nmrresource
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Acid
Hydrophilic
Sequence,Bacterial
Proteins,Hydrophobic
Sequence
Structure,Recombinant
Data,Nuclear
Magnetic
and
Amino
Interactions,Inactivation,Mercury,Metabolic,Micelles,Molecular
Proteins,Secondary
Resonance,Protein
Transport
Proteins,Biomolecular,Cation
AcidHydrophilicSequence,BacterialProteins,HydrophobicSequenceStructure,RecombinantData,NuclearMagneticandAminoInteractions,Inactivation,Mercury,Metabolic,Micelles,MolecularProteins,SecondaryResonance,ProteinTransportProteins,Biomolecular,Cation
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1A small region in phosducin inhibits G-protein betagamma-subunit function
K. Bluml, W. Schnepp, S. Schroder, M. Beyermann, M. Macias, H. Oschkinat, and M. Lohse. EMBO J, 16 (16): 4908-15 (August 1997)Bluml, K Schnepp, W Schroder, S Beyermann, M Macias, M Oschkinat, H Lohse, M J Research Support, Non-U.S. Gov't England The EMBO journal EMBO J. 1997 Aug 15;16(16):4908-15..
14 years ago by @pharmawuerz
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Binding
Spectroscopy
Structure,
Phosphoproteins/*chemistry/genetics/metabolism/*pharmacology
Secondary
Fragments/chemistry/metabolism/pharmacology
&
Phosphohydrolases/antagonists
Data
Sequence
Protein
Animals
inhibitors/metabolism
Blotting,
X-Ray
Resonance
Mutation
Fusion
Models,
Regulators
Acid
GTP
Proteins/*chemistry/genetics/metabolism/*pharmacology
Crystallography,
Proteins/*antagonists
Eye
Molecular
Proteins/chemistry/metabolism/pharmacology
Western
Magnetic
GTP-Binding
Amino
Kinases/genetics/metabolism
Peptide
Recombinant
BindingSpectroscopyStructure,Phosphoproteins/*chemistry/genetics/metabolism/*pharmacologySecondaryFragments/chemistry/metabolism/pharmacology&Phosphohydrolases/antagonistsDataSequenceProteinAnimalsinhibitors/metabolismBlotting,X-RayResonanceMutationFusionModels,RegulatorsAcidGTPProteins/*chemistry/genetics/metabolism/*pharmacologyCrystallography,Proteins/*antagonistsEyeMolecularProteins/chemistry/metabolism/pharmacologyWesternMagneticGTP-BindingAminoKinases/genetics/metabolismPeptideRecombinant
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1Angstr�ms and calories.
J. Janin. Structure, 5 (4): 473--479 (April 1997)
16 years ago by @hake
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Nucleoside-Diphosphate
Structure,
Trans,
Dictyostelium,
Spectroscopy,
Solvents,
Base
Diphosphates,
Humans,
Molecular,
Entropy,
DNA,
DNA
Thermodynamics,
Ribonucleases,
Resonance
Sequence,
X-Ray,
Factual,
Animals,
Bacterial
Transcription
Complementary,
Research
Primers,
Data,
Solutions,
Factors,
ding
Kinase,
Magnetic
Homology,
Confocal,
Protons,
Crystallization,
Electrostatics,
Cell
Binding
Calorimetry,
Sequence
Zidovudine,
Support,
Acid,
Monomeric
Protein
9115438
formed,
Line,
Microscopy,
Models,
Bin,
Acid
Binding,
Mitochondria,
Gov't,
Crystallography,
Secondary,
Databases,
Conformation,
Molecular
Kinetics,
Proteins,
Non-U.S.
GTP-Binding
Amino
Sites,
Nucleoside-DiphosphateStructure,Trans,Dictyostelium,Spectroscopy,Solvents,BaseDiphosphates,Humans,Molecular,Entropy,DNA,DNAThermodynamics,Ribonucleases,ResonanceSequence,X-Ray,Factual,Animals,BacterialTranscriptionComplementary,ResearchPrimers,Data,Solutions,Factors,dingKinase,MagneticHomology,Confocal,Protons,Crystallization,Electrostatics,CellBindingCalorimetry,SequenceZidovudine,Support,Acid,MonomericProtein9115438formed,Line,Microscopy,Models,Bin,AcidBinding,Mitochondria,Gov't,Crystallography,Secondary,Databases,Conformation,MolecularKinetics,Proteins,Non-U.S.GTP-BindingAminoSites,
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1Conformational changes induced by a single amino acid substitution in the trans-membrane domain of \Vpu\: implications for \HIV\-1 susceptibility to channel blocking drugs
S. Park, and S. Opella. Protein Sci., 16 (10): 2205--2215 (October 2007)
8 years ago by @nmrresource
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Acid
Sequence,Amino
Immunodeficiency
Regulatory
Conformation,Protein
Sequence
Channels,Micelles,Models,Molecular,Molecular
Proteins
Accessory
Data,Nuclear
Virus
Proteins,Ion
Magnetic
and
Agents,Biomolecular,HIV-1,Human
Amino
Resonance,Protein
Structure,Rimantadine,Tertiary,Viral
Substitution,Anti-HIV
AcidSequence,AminoImmunodeficiencyRegulatoryConformation,ProteinSequenceChannels,Micelles,Models,Molecular,MolecularProteinsAccessoryData,NuclearVirusProteins,IonMagneticandAgents,Biomolecular,HIV-1,HumanAminoResonance,ProteinStructure,Rimantadine,Tertiary,ViralSubstitution,Anti-HIV
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1Dilute spin-exchange assignment of solid-state \NMR\ spectra of oriented proteins: acetylcholine \M\2 in bilayers
F. Marassi, J. Gesell, A. Valente, Y. Kim, M. Oblatt-Montal, M. Montal, and S. Opella. J. Biomol. NMR, 14 (2): 141--148 (June 1999)
8 years ago by @nmrresource
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Data,Muscarinic,Muscarinic
Isotopes,Nuclear
Acid
Magnetic
bilayers,Molecular
Fragments,Protein
Amino
Resonance,Peptide
Sequence
M2,Nitrogen
Conformation,Receptor,Receptors
Sequence,Biomolecular,Lipid
Data,Muscarinic,MuscarinicIsotopes,NuclearAcidMagneticbilayers,MolecularFragments,ProteinAminoResonance,PeptideSequenceM2,NitrogenConformation,Receptor,ReceptorsSequence,Biomolecular,Lipid
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1Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy
Y. Hashimoto, K. Toma, J. Nishikido, K. Yamamoto, K. Haneda, T. Inazu, K. Valentine, and S. Opella. Biochemistry, 38 (26): 8377--8384 (June 1999)
8 years ago by @nmrresource
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Acid
Acetylglucosamine,Amino
Conformation,Carbohydrate
Fragments,Protein
Resonance,Peptide
Sequence
Structure,Secondary,Structure-Activity
bilayers,Micelles,Molecular
Data,Nuclear
Relationship,Thermodynamics,X-Ray
Magnetic
Sequence,Animals,Biomolecular,Calcitonin,Carbohydrate
Sequence,Crystallography,Eels,Glycosylation,Lipid
AcidAcetylglucosamine,AminoConformation,CarbohydrateFragments,ProteinResonance,PeptideSequenceStructure,Secondary,Structure-Activitybilayers,Micelles,MolecularData,NuclearRelationship,Thermodynamics,X-RayMagneticSequence,Animals,Biomolecular,Calcitonin,CarbohydrateSequence,Crystallography,Eels,Glycosylation,Lipid
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1Functional characterization and \NMR\ spectroscopy on full-length \Vpu\ from \HIV\-1 prepared by total chemical synthesis
G. Kochendoerfer, D. Jones, S. Lee, M. Oblatt-Montal, S. Opella, and M. Montal. J. Am. Chem. Soc., 126 (8): 2439--2446 (March 2004)
8 years ago by @nmrresource
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Acid
Immunodeficiency
Proteins,Viral
Regulatory
Sequence
bilayers,Micelles,Molecular
Proteins
Accessory
Data,Nuclear
Virus
Resonance,Recombinant
Proteins,Ion
Magnetic
Sequence,Biomolecular,HIV-1,Human
and
Amino
Channels,Lipid
AcidImmunodeficiencyProteins,ViralRegulatorySequencebilayers,Micelles,MolecularProteinsAccessoryData,NuclearVirusResonance,RecombinantProteins,IonMagneticSequence,Biomolecular,HIV-1,HumanandAminoChannels,Lipid
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1Impact of histidine residues on the transmembrane helices of viroporins
Y. Wang, S. Park, Y. Tian, and S. Opella. Mol. Membr. Biol., 30 (7): 360--369 (November 2013)
8 years ago by @nmrresource
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A
Proteins,Molecular
Acid
Immunodeficiency
Motifs,Amino
virus,Membrane
Proteins,Viral
Mutation,Protein
Regulatory
Sequence
Proteins
Accessory
Data,Nuclear
Virus
Matrix
Magnetic
Resonance,Point
Structure,Secondary,Viral
and
Amino
Sequence,Biomolecular,HIV-1,Histidine,Human
Proteins,Influenza
AProteins,MolecularAcidImmunodeficiencyMotifs,Aminovirus,MembraneProteins,ViralMutation,ProteinRegulatorySequenceProteinsAccessoryData,NuclearVirusMatrixMagneticResonance,PointStructure,Secondary,ViralandAminoSequence,Biomolecular,HIV-1,Histidine,HumanProteins,Influenza
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1Lanthanide ions bind specifically to an added "\EF\-hand" and orient a membrane protein in micelles for solution \NMR\ spectroscopy
C. Ma, and S. Opella. J. Magn. Reson., 146 (2): 381--384 (October 2000)
8 years ago by @nmrresource
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Data,Nuclear
Earth
Acid
Magnetic
Resonance,Rare
Proteins,Metals,Micelles,Molecular
Amino
Sequence
Sequence,Biomolecular,HIV-1,Membrane
Data,NuclearEarthAcidMagneticResonance,RareProteins,Metals,Micelles,MolecularAminoSequenceSequence,Biomolecular,HIV-1,Membrane
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1Local and global dynamics of the \G\ protein-coupled receptor \CXCR\1
S. Park, F. Casagrande, B. Das, L. Albrecht, M. Chu, and S. Opella. Biochemistry, 50 (12): 2371--2380 (March 2011)
8 years ago by @nmrresource
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Data,Nuclear
Acid
Magnetic
Conformation,Receptors,Rotation
bilayers,Magnetics,Micelles,Models,Molecular,Molecular
Amino
Sequence
Resonance,Protein
Sequence,Biomolecular,Diffusion,Humans,Interleukin-8A,Lipid
Data,NuclearAcidMagneticConformation,Receptors,Rotationbilayers,Magnetics,Micelles,Models,Molecular,MolecularAminoSequenceResonance,ProteinSequence,Biomolecular,Diffusion,Humans,Interleukin-8A,Lipid
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1Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for \NMR\ structure determination
S. Park, B. Das, A. De Angelis, M. Scrima, and S. Opella. J Phys Chem B, 114 (44): 13995--14003 (November 2010)
8 years ago by @nmrresource
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Phenomena,Biomolecular,Capsid
Resonance,Phospholipids,Protein
Acid
Processes,Membrane
Structure,Rotation,Tertiary
Proteins,Diffusion,Lipid
Sequence
Proteins,Models,Molecular,Molecular
bilayers,Magnetics,Mechanical
Data,Nuclear
Magnetic
M13,Biomechanical
Sequence,Bacteriophage
Amino
Phenomena,Biomolecular,CapsidResonance,Phospholipids,ProteinAcidProcesses,MembraneStructure,Rotation,TertiaryProteins,Diffusion,LipidSequenceProteins,Models,Molecular,Molecularbilayers,Magnetics,MechanicalData,NuclearMagneticM13,BiomechanicalSequence,BacteriophageAmino
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1Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (\HQA\)
S. Park, V. Wang, J. Radoicic, A. De Angelis, S. Berkamp, and S. Opella. J. Biomol. NMR, 61 (3-4): 185--196 (April 2015)
8 years ago by @nmrresource
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Acid
Sequence,Amino
Acids,Binding
Spin
Alanine,Amino
Sites,Biomolecular,Electron
Sequence
Proteins,Models,Molecular,Molecular
Data,Nuclear
Substitution,Amino
Magnetic
Resonance,Propionates,Protein
Resonance
Binding,Protein
coli,Hydroxyquinolines,Interleukin-8,Interleukin-8A,Membrane
Structure,Receptors,Tertiary
Spectroscopy,Escherichia
AcidSequence,AminoAcids,BindingSpinAlanine,AminoSites,Biomolecular,ElectronSequenceProteins,Models,Molecular,MolecularData,NuclearSubstitution,AminoMagneticResonance,Propionates,ProteinResonanceBinding,Proteincoli,Hydroxyquinolines,Interleukin-8,Interleukin-8A,MembraneStructure,Receptors,TertiarySpectroscopy,Escherichia
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1Selectivity in heavy metal- binding to peptides and proteins
T. DeSilva, G. Veglia, F. Porcelli, A. Prantner, and S. Opella. Biopolymers, 64 (4): 189--197 (August 2002)
8 years ago by @nmrresource
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Binding,Proteins
Data,Nuclear
Acid
Magnetic
Dichroism,Heavy,Metals,Models,Molecular,Molecular
Resonance,Peptides,Protein
Amino
Sequence
Sequence,Biomolecular,Biopolymers,Circular
Binding,ProteinsData,NuclearAcidMagneticDichroism,Heavy,Metals,Models,Molecular,MolecularResonance,Peptides,ProteinAminoSequenceSequence,Biomolecular,Biopolymers,Circular
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1Simultaneous assignment and structure determination of a membrane protein from \NMR\ orientational restraints
F. Marassi, and S. Opella. Protein Sci., 12 (3): 403--411 (March 2003)
8 years ago by @nmrresource
show all tags
Data,Nuclear
Sequence,Biomolecular,Capsid
Acid
Magnetic
Proteins,Membrane
Amino
Sequence
Proteins,Models,Molecular,Molecular
Resonance,Protein
Conformation
Data,NuclearSequence,Biomolecular,CapsidAcidMagneticProteins,MembraneAminoSequenceProteins,Models,Molecular,MolecularResonance,ProteinConformation
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1Single tryptophan and tyrosine comparisons in the \N\-terminal and \C\-terminal interface regions of transmembrane \GWALP\ peptides
N. Gleason, D. Greathouse, C. Grant, S. Opella, and R. Koeppe. J Phys Chem B, 117 (44): 13786--13794 (November 2013)
8 years ago by @nmrresource
show all tags
Data,Nuclear
Acid
Hydrophilic
Sequence,Biomolecular,Hydrophobic
Magnetic
bilayers,Molecular
Resonance,Peptides,Protein
and
Amino
Sequence
Interactions,Lipid
Structure,Secondary,Tryptophan,Tyrosine,Water
Data,NuclearAcidHydrophilicSequence,Biomolecular,HydrophobicMagneticbilayers,MolecularResonance,Peptides,ProteinandAminoSequenceInteractions,LipidStructure,Secondary,Tryptophan,Tyrosine,Water
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1Solid-state \NMR\ and membrane proteins
S. Opella. J. Magn. Reson., (April 2015)
8 years ago by @nmrresource
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Proteins,Molecular
Resonance,Phospholipids,Protein
Labels,Structure
Acid
shift
coupling,Lipid
Sequence
determination
Conformation,Spin
Sites,Biomolecular,Chemical
bilayers,Magic
Data,Nuclear
Sequence,Bilayers,Binding
Magnetic
angle
anisotropy,Dipolar
Amino
spinning,Membrane
Binding,Protein
Proteins,MolecularResonance,Phospholipids,ProteinLabels,StructureAcidshiftcoupling,LipidSequencedeterminationConformation,SpinSites,Biomolecular,Chemicalbilayers,MagicData,NuclearSequence,Bilayers,BindingMagneticangleanisotropy,DipolarAminospinning,MembraneBinding,Protein
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1Structural basis of the temperature transition of \Pf\1 bacteriophage
D. Thiriot, A. Nevzorov, and S. Opella. Protein Sci., 14 (4): 1064--1070 (April 2005)
8 years ago by @nmrresource
show all tags
Data,Nuclear
Proteins,Molecular
Sequence,Biomolecular,Capsid
Acid
Magnetic
Resonance,Temperature
Amino
Sequence
Data,NuclearProteins,MolecularSequence,Biomolecular,CapsidAcidMagneticResonance,TemperatureAminoSequence
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1Structure and dynamics of the antibiotic peptide \PGLa\ in membranes by solution and solid-state nuclear magnetic resonance spectroscopy
B. Bechinger, M. Zasloff, and S. Opella. Biophys. J., 74 (2 Pt 1): 981--987 (February 1998)
8 years ago by @nmrresource
show all tags
Cationic
Acid
Resonance,Peptides,Phosphatidylethanolamines,Phosphatidylglycerols,Protein
Sequence,Antimicrobial
Magnetic
Structure,Secondary,Solutions
Amino
Conformation,Protein
Sequence
Peptides,Biomolecular,Lipid
Data,Nitrogen,Nuclear
bilayers,Micelles,Molecular
CationicAcidResonance,Peptides,Phosphatidylethanolamines,Phosphatidylglycerols,ProteinSequence,AntimicrobialMagneticStructure,Secondary,SolutionsAminoConformation,ProteinSequencePeptides,Biomolecular,LipidData,Nitrogen,Nuclearbilayers,Micelles,Molecular
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1Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state \NMR\ spectroscopy
A. De Angelis, S. Howell, A. Nevzorov, and S. Opella. J. Am. Chem. Soc., 128 (37): 12256--12267 (September 2006)
8 years ago by @nmrresource
show all tags
Data,Nuclear
Resonance,Phospholipids,Protein
Acid
Magnetic
Structure,Secondary
bilayers,Membrane
Amino
Sequence
Proteins,Models,Molecular,Molecular
Sequence,Biomolecular,Lipid
Data,NuclearResonance,Phospholipids,ProteinAcidMagneticStructure,Secondarybilayers,MembraneAminoSequenceProteins,Models,Molecular,MolecularSequence,Biomolecular,Lipid
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1\HIV\-1 \Vpu\ protein antagonizes innate restriction factor \BST\-2 via lipid-embedded helix-helix interactions

1\NMR\ structure determination of a membrane protein with two transmembrane helices in micelles: \MerF\ of the bacterial mercury detoxification system

1A small region in phosducin inhibits G-protein betagamma-subunit function

1Angstr�ms and calories.

1Conformational changes induced by a single amino acid substitution in the trans-membrane domain of \Vpu\: implications for \HIV\-1 susceptibility to channel blocking drugs

1Dilute spin-exchange assignment of solid-state \NMR\ spectra of oriented proteins: acetylcholine \M\2 in bilayers

1Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy

1Functional characterization and \NMR\ spectroscopy on full-length \Vpu\ from \HIV\-1 prepared by total chemical synthesis

1Impact of histidine residues on the transmembrane helices of viroporins

1Lanthanide ions bind specifically to an added "\EF\-hand" and orient a membrane protein in micelles for solution \NMR\ spectroscopy

1Local and global dynamics of the \G\ protein-coupled receptor \CXCR\1

1Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for \NMR\ structure determination

1Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (\HQA\)

1Selectivity in heavy metal- binding to peptides and proteins

1Simultaneous assignment and structure determination of a membrane protein from \NMR\ orientational restraints

1Single tryptophan and tyrosine comparisons in the \N\-terminal and \C\-terminal interface regions of transmembrane \GWALP\ peptides

1Solid-state \NMR\ and membrane proteins

1Structural basis of the temperature transition of \Pf\1 bacteriophage

1Structure and dynamics of the antibiotic peptide \PGLa\ in membranes by solution and solid-state nuclear magnetic resonance spectroscopy

1Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state \NMR\ spectroscopy

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publications (hide)23
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