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1Properties of membrane-incorporated \WALP\ peptides that are anchored on only one end
J. Rankenberg, V. Vostrikov, D. Greathouse, C. Grant, S. Opella, и R. Koeppe. Biochemistry, 51 (50): 10066--10074 (декабря 2012)
8 лет назад , @nmrresource
Acid
Hydrophilic
Magnetic
bilayers,Nuclear
Structure,Secondary,Tryptophan
Resonance,Oligopeptides,Peptides,Phosphatidylcholines,Protein
Sequence,Biomolecular,Dimyristoylphosphatidylcholine,Hydrophobic
and
Amino
Interactions,Lipid
AcidHydrophilicMagneticbilayers,NuclearStructure,Secondary,TryptophanResonance,Oligopeptides,Peptides,Phosphatidylcholines,ProteinSequence,Biomolecular,Dimyristoylphosphatidylcholine,HydrophobicandAminoInteractions,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, и S. Opella. J Phys Chem B, 114 (44): 13995--14003 (ноября 2010)
8 лет назад , @nmrresource
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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1Selectivity in heavy metal- binding to peptides and proteins
T. DeSilva, G. Veglia, F. Porcelli, A. Prantner, и S. Opella. Biopolymers, 64 (4): 189--197 (августа 2002)
8 лет назад , @nmrresource
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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1Local and global dynamics of the \G\ protein-coupled receptor \CXCR\1
S. Park, F. Casagrande, B. Das, L. Albrecht, M. Chu, и S. Opella. Biochemistry, 50 (12): 2371--2380 (марта 2011)
8 лет назад , @nmrresource
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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1Lanthanide ions bind specifically to an added "\EF\-hand" and orient a membrane protein in micelles for solution \NMR\ spectroscopy
C. Ma, и S. Opella. J. Magn. Reson., 146 (2): 381--384 (октября 2000)
8 лет назад , @nmrresource
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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1Structure and dynamics of the antibiotic peptide \PGLa\ in membranes by solution and solid-state nuclear magnetic resonance spectroscopy
B. Bechinger, M. Zasloff, и S. Opella. Biophys. J., 74 (2 Pt 1): 981--987 (февраля 1998)
8 лет назад , @nmrresource
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, и S. Opella. J. Am. Chem. Soc., 128 (37): 12256--12267 (сентября 2006)
8 лет назад , @nmrresource
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\NMR\ structure determination of a membrane protein with two transmembrane helices in micelles: \MerF\ of the bacterial mercury detoxification system
S. Howell, M. Mesleh, и S. Opella. Biochemistry, 44 (13): 5196--5206 (апреля 2005)
8 лет назад , @nmrresource
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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1Simultaneous assignment and structure determination of a membrane protein from \NMR\ orientational restraints
F. Marassi, и S. Opella. Protein Sci., 12 (3): 403--411 (марта 2003)
8 лет назад , @nmrresource
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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1Impact of histidine residues on the transmembrane helices of viroporins
Y. Wang, S. Park, Y. Tian, и S. Opella. Mol. Membr. Biol., 30 (7): 360--369 (ноября 2013)
8 лет назад , @nmrresource
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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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, и S. Opella. Protein Sci., 16 (10): 2205--2215 (октября 2007)
8 лет назад , @nmrresource
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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1Three-dimensional structure of the transmembrane domain of \Vpu\ from \HIV\-1 in aligned phospholipid bicelles
S. Park, A. De Angelis, A. Nevzorov, C. Wu, и S. Opella. Biophys. J., 91 (8): 3032--3042 (октября 2006)
8 лет назад , @nmrresource
Acid
Immunodeficiency
bilayers,Molecular
Regulatory
Sequence
Proteins,Lipid
Proteins
Accessory
Data,Nuclear
Virus
Magnetic
Resonance,Peptides,Phospholipids,Protein
Sequence,Biomolecular,HIV-1,Human
and
Structure,Secondary,Tertiary,Viral
Amino
AcidImmunodeficiencybilayers,MolecularRegulatorySequenceProteins,LipidProteinsAccessoryData,NuclearVirusMagneticResonance,Peptides,Phospholipids,ProteinSequence,Biomolecular,HIV-1,HumanandStructure,Secondary,Tertiary,ViralAmino
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1The structure of the mercury transporter \MerF\ in phospholipid bilayers: a large conformational rearrangement results from \N\-terminal truncation
G. Lu, Y. Tian, N. Vora, F. Marassi, и S. Opella. J. Am. Chem. Soc., 135 (25): 9299--9302 (июня 2013)
8 лет назад , @nmrresource
Data,Nuclear
Resonance,Phospholipids,Protein
Acid
Magnetic
bilayers,Models,Molecular,Molecular
Sequence,Bacterial
Amino
Sequence
Transport
Proteins,Biomolecular,Cation
Conformation
Proteins,Lipid
Data,NuclearResonance,Phospholipids,ProteinAcidMagneticbilayers,Models,Molecular,MolecularSequence,BacterialAminoSequenceTransportProteins,Biomolecular,CationConformationProteins,Lipid
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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, и R. Koeppe. J Phys Chem B, 117 (44): 13786--13794 (ноября 2013)
8 лет назад , @nmrresource
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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1Tyrosine replacing tryptophan as an anchor in \GWALP\ peptides
N. Gleason, V. Vostrikov, D. Greathouse, C. Grant, S. Opella, и R. Koeppe. Biochemistry, 51 (10): 2044--2053 (марта 2012)
8 лет назад , @nmrresource
Simulation,Molecular
Acid
Hydrophilic
Resonance,Peptides,Protein
bilayers,Membrane
Structure,Secondary,Spectrometry,Tryptophan,Tyrosine
Sequence
Proteins,Models,Molecular,Molecular
Interactions,Lipid
Dichroism,Fluorescence,Hydrophobic
Data,Nuclear
Dynamics
Magnetic
and
Sequence,Biomolecular,Circular
Amino
Simulation,MolecularAcidHydrophilicResonance,Peptides,Proteinbilayers,MembraneStructure,Secondary,Spectrometry,Tryptophan,TyrosineSequenceProteins,Models,Molecular,MolecularInteractions,LipidDichroism,Fluorescence,HydrophobicData,NuclearDynamicsMagneticandSequence,Biomolecular,CircularAmino
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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, и M. Montal. J. Am. Chem. Soc., 126 (8): 2439--2446 (марта 2004)
8 лет назад , @nmrresource
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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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, и J. Guatelli. J. Biol. Chem., 287 (1): 58--67 (января 2012)
8 лет назад , @nmrresource
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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1Solid-state \NMR\ and membrane proteins
S. Opella. J. Magn. Reson., (апреля 2015)
8 лет назад , @nmrresource
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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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, и S. Opella. J. Biomol. NMR, 14 (2): 141--148 (июня 1999)
8 лет назад , @nmrresource
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
копироватьудалитьдобавить публикацию в буфер
1Structural basis of the temperature transition of \Pf\1 bacteriophage
D. Thiriot, A. Nevzorov, и S. Opella. Protein Sci., 14 (4): 1064--1070 (апреля 2005)
8 лет назад , @nmrresource
Data,Nuclear
Proteins,Molecular
Sequence,Biomolecular,Capsid
Acid
Magnetic
Resonance,Temperature
Amino
Sequence
Data,NuclearProteins,MolecularSequence,Biomolecular,CapsidAcidMagneticResonance,TemperatureAminoSequence
копироватьудалитьдобавить публикацию в буфер
1Improved chemical shift prediction by \Rosetta\ conformational sampling
Y. Tian, S. Opella, и F. Marassi. J. Biomol. NMR, 54 (3): 237--243 (ноября 2012)
8 лет назад , @nmrresource
Sequence,Biomolecular,Membrane
Proteins,Nuclear
Acid
Magnetic
Conformation,Proteins,Software
Amino
Resonance,Protein
Sequence,Biomolecular,MembraneProteins,NuclearAcidMagneticConformation,Proteins,SoftwareAminoResonance,Protein
копироватьудалитьдобавить публикацию в буфер
1Spastic diplegia and periventricular white matter abnormalities in 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency, a defect of isoleucine metabolism: differential diagnosis with hypoxic-ischemic brain diseases.
B. Poll-The, R. Wanders, J. Ruiter, R. Ofman, C. Majoie, P. Barth, и M. Duran. Mol Genet Metab, 81 (4): 295--299 (апреля 2004)
10 лет назад , @ar0berts
Humans;
Mutational
Cerebral
Diagnosis,
Palsy;
Leukomalacia,
Analysis;
DNA
Resonance
Mutation
Periventricular;
Infant,
Inborn
Acid
Multiple;
Metabolism,
Abnormalities,
Isoleucine;
Male;
Alcohol
Newborn;
Differential;
Oxidoreductases;
Anoxia;
Infant;
Magnetic
Amino
Imaging;
Errors;
Humans;MutationalCerebralDiagnosis,Palsy;Leukomalacia,Analysis;DNAResonanceMutationPeriventricular;Infant,InbornAcidMultiple;Metabolism,Abnormalities,Isoleucine;Male;AlcoholNewborn;Differential;Oxidoreductases;Anoxia;Infant;MagneticAminoImaging;Errors;
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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, и M. Lohse. EMBO J, 16 (16): 4908-15 (августа 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 лет назад , @pharmawuerz
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 (апреля 1997)
16 лет назад , @hake
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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1Properties of membrane-incorporated \WALP\ peptides that are anchored on only one end

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

1Selectivity in heavy metal- binding to peptides and proteins

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

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

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

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

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

1Impact of histidine residues on the transmembrane helices of viroporins

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

1Three-dimensional structure of the transmembrane domain of \Vpu\ from \HIV\-1 in aligned phospholipid bicelles

1The structure of the mercury transporter \MerF\ in phospholipid bilayers: a large conformational rearrangement results from \N\-terminal truncation

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

1Tyrosine replacing tryptophan as an anchor in \GWALP\ peptides

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

1\HIV\-1 \Vpu\ protein antagonizes innate restriction factor \BST\-2 via lipid-embedded helix-helix interactions

1Solid-state \NMR\ and membrane proteins

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

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

1Improved chemical shift prediction by \Rosetta\ conformational sampling

1Spastic diplegia and periventricular white matter abnormalities in 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency, a defect of isoleucine metabolism: differential diagnosis with hypoxic-ischemic brain diseases.

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

1Angstr�ms and calories.

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