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Volumn 16, Issue 5, 2006, Pages 618-623

Molecular interactions investigated by multi-dimensional solid-state NMR

Author keywords

[No Author keywords available]

Indexed keywords

GLOBULAR PROTEIN; MEMBRANE PROTEIN;

EID: 33749049148     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2006.08.003     Document Type: Review
Times cited : (60)

References (57)
  • 1
    • 32344445231 scopus 로고    scopus 로고
    • NMR studies of protein interactions
    • Takeuchi K., and Wagner G. NMR studies of protein interactions. Curr Opin Struct Biol 16 (2006) 109-117
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 109-117
    • Takeuchi, K.1    Wagner, G.2
  • 3
    • 0030272669 scopus 로고    scopus 로고
    • High-resolution NMR of biological solids
    • McDowell L.M., and Schaefer J. High-resolution NMR of biological solids. Curr Opin Struct Biol 6 (1996) 624-629
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 624-629
    • McDowell, L.M.1    Schaefer, J.2
  • 4
    • 0037195278 scopus 로고    scopus 로고
    • Rotational-Echo double resonance characterization of the effects of vancomycin on cell wall synthesis in Staphylococcus aureus
    • Cegelski L., Kim S.J., Hing A.W., Studelska D.R., O'Connor R.D., Mehta A.K., and Schaefer J. Rotational-Echo double resonance characterization of the effects of vancomycin on cell wall synthesis in Staphylococcus aureus. Biochemistry 41 (2002) 13053-13058
    • (2002) Biochemistry , vol.41 , pp. 13053-13058
    • Cegelski, L.1    Kim, S.J.2    Hing, A.W.3    Studelska, D.R.4    O'Connor, R.D.5    Mehta, A.K.6    Schaefer, J.7
  • 5
    • 22144499552 scopus 로고    scopus 로고
    • Solid-state NMR in drug design and discovery for membrane-embedded targets
    • Watts A. Solid-state NMR in drug design and discovery for membrane-embedded targets. Nat Rev Drug Discov 4 (2005) 555-568
    • (2005) Nat Rev Drug Discov , vol.4 , pp. 555-568
    • Watts, A.1
  • 6
    • 33745315198 scopus 로고
    • Nuclear magnetic resonance spectra from a crystal rotated at high speed
    • Andrew E.R., Bradbury A., and Eades R.G. Nuclear magnetic resonance spectra from a crystal rotated at high speed. Nature 182 (1958) 1659
    • (1958) Nature , vol.182 , pp. 1659
    • Andrew, E.R.1    Bradbury, A.2    Eades, R.G.3
  • 8
    • 2342482988 scopus 로고    scopus 로고
    • Identification of NH.N hydrogen bonds by magic angle spinning solid state NMR in a double-stranded RNA associated with myotonic dystrophy
    • Leppert J., Urbinati C.R., Hafner S., Ohlenschlager O., Swanson M.S., Gorlach M., and Ramachandran R. Identification of NH.N hydrogen bonds by magic angle spinning solid state NMR in a double-stranded RNA associated with myotonic dystrophy. Nucleic Acids Res 32 (2004) 1177-1183
    • (2004) Nucleic Acids Res , vol.32 , pp. 1177-1183
    • Leppert, J.1    Urbinati, C.R.2    Hafner, S.3    Ohlenschlager, O.4    Swanson, M.S.5    Gorlach, M.6    Ramachandran, R.7
  • 10
    • 4744372317 scopus 로고    scopus 로고
    • Characterization of protein-ligand Interactions by high-resolution solid-state NMR spectroscopy
    • Zech S.G., Olejniczak E., Hajduk P., Mack J., and McDermott A.E. Characterization of protein-ligand Interactions by high-resolution solid-state NMR spectroscopy. J Am Chem Soc 126 (2004) 13948-13953
    • (2004) J Am Chem Soc , vol.126 , pp. 13948-13953
    • Zech, S.G.1    Olejniczak, E.2    Hajduk, P.3    Mack, J.4    McDermott, A.E.5
  • 11
    • 26444481982 scopus 로고    scopus 로고
    • Observation of ligand binding to cytochrome P450 BM-3 by means of solid-state NMR spectroscopy
    • Jovanovic T., and McDermott A.E. Observation of ligand binding to cytochrome P450 BM-3 by means of solid-state NMR spectroscopy. J Am Chem Soc 127 (2005) 13816-13821
    • (2005) J Am Chem Soc , vol.127 , pp. 13816-13821
    • Jovanovic, T.1    McDermott, A.E.2
  • 12
    • 25844447810 scopus 로고    scopus 로고
    • Thermal equilibrium of high- and low-spin forms of cytochrome P450 BM-3: repositioning of the substrate?
    • The authors employ 2D ssNMR to study the binding characteristics of a cytochrome P450 substrate as a function of temperature. They propose a temperature-dependent ligand position, a view that is supported by recent MD simulations (Ravindranathan et al., J Am Chem Soc 2006, 128:5786).
    • Jovanovic T., Farid R., Friesner R.A., and McDermott A.E. Thermal equilibrium of high- and low-spin forms of cytochrome P450 BM-3: repositioning of the substrate?. J Am Chem Soc 127 (2005) 13548-13552. The authors employ 2D ssNMR to study the binding characteristics of a cytochrome P450 substrate as a function of temperature. They propose a temperature-dependent ligand position, a view that is supported by recent MD simulations (Ravindranathan et al., J Am Chem Soc 2006, 128:5786).
    • (2005) J Am Chem Soc , vol.127 , pp. 13548-13552
    • Jovanovic, T.1    Farid, R.2    Friesner, R.A.3    McDermott, A.E.4
  • 13
    • 4244050504 scopus 로고    scopus 로고
    • Solid-state NMR sequential resonance assignments and conformational analysis of the 2×10.4 kDa dimeric form of the Bacillus subtilis protein Crh
    • Böckmann A., Lange A., Galinier A., Luca S., Giraud N., Heise H., Juy M., Montserret R., Penin F., and Baldus M. Solid-state NMR sequential resonance assignments and conformational analysis of the 2×10.4 kDa dimeric form of the Bacillus subtilis protein Crh. J Biomol NMR 27 (2003) 323-339
    • (2003) J Biomol NMR , vol.27 , pp. 323-339
    • Böckmann, A.1    Lange, A.2    Galinier, A.3    Luca, S.4    Giraud, N.5    Heise, H.6    Juy, M.7    Montserret, R.8    Penin, F.9    Baldus, M.10
  • 14
    • 11444258696 scopus 로고    scopus 로고
    • Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. Resonance assignments of differentially enriched Escherichia thioredoxin reassembled by fragment complementation
    • Marulanda D., Tasayco M.L., McDermott A., Cataldi M., Arriaran V., and Polenova T. Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. Resonance assignments of differentially enriched Escherichia thioredoxin reassembled by fragment complementation. J Am Chem Soc 126 (2004) 16608-16620
    • (2004) J Am Chem Soc , vol.126 , pp. 16608-16620
    • Marulanda, D.1    Tasayco, M.L.2    McDermott, A.3    Cataldi, M.4    Arriaran, V.5    Polenova, T.6
  • 15
    • 0037047148 scopus 로고    scopus 로고
    • H-1 and C-13 MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin
    • Creemers A.F.L., Kiihne S., Bovee-Geurts P.H.M., DeGrip W.J., Lugtenburg J., and de Groot H.J.M. H-1 and C-13 MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin. Proc Natl Acad Sci USA 99 (2002) 9101-9106
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9101-9106
    • Creemers, A.F.L.1    Kiihne, S.2    Bovee-Geurts, P.H.M.3    DeGrip, W.J.4    Lugtenburg, J.5    de Groot, H.J.M.6
  • 18
    • 33644613761 scopus 로고    scopus 로고
    • NMR studies of organic polymorphs and solvates
    • Harris R.K. NMR studies of organic polymorphs and solvates. Analyst 131 (2006) 351-373
    • (2006) Analyst , vol.131 , pp. 351-373
    • Harris, R.K.1
  • 19
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • This paper establishes a relationship between fibril morphology and molecular structure for fibrils formed by the 40-residue β-amyloid peptide of Alzheimer's disease (Aβ(1-40)) using 2D ssNMR. In addition, Petkova et al. show that different Aβ(1-40) fibril morphologies have significantly different toxicities in neuronal cell cultures.
    • Petkova A.T., Leapman R.D., Guo Z., Yau W.-M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 307 (2005) 262-265. This paper establishes a relationship between fibril morphology and molecular structure for fibrils formed by the 40-residue β-amyloid peptide of Alzheimer's disease (Aβ(1-40)) using 2D ssNMR. In addition, Petkova et al. show that different Aβ(1-40) fibril morphologies have significantly different toxicities in neuronal cell cultures.
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 20
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • Petkova A.T., Yau W.M., and Tycko R. Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils. Biochemistry 45 (2006) 498-512
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 21
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
    • This paper describes the use of 2D and 3D ssNMR to study structure and dynamics of full length α-synuclein fibrils (in the presence of soluble protein monomers) and identifies two different fibril forms using 2D ssNMR and electron microscopy. Reverse labeling was crucial to obtain sequential resonance assignments in this 140 aa protein.
    • Heise H., Hoyer W., Becker S., Andronesi O.C., Riedel D., and Baldus M. Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR. Proc Natl Acad Sci USA 102 (2005) 15871-15876. This paper describes the use of 2D and 3D ssNMR to study structure and dynamics of full length α-synuclein fibrils (in the presence of soluble protein monomers) and identifies two different fibril forms using 2D ssNMR and electron microscopy. Reverse labeling was crucial to obtain sequential resonance assignments in this 140 aa protein.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 22
    • 20444458341 scopus 로고    scopus 로고
    • Correlation of structural elements and infectivity of the HET-s prion
    • The authors employ 2D ssNMR to determine the sequence-specific positions of amyloid fibril secondary structure elements of HET-s(218-289) fibrils. Structure-based mutagenesis reveals that the fibril conformation is the functional and infectious entity of the HET-s prion.
    • Ritter C., Maddelein M.-L., Siemer A.B., Luhrs T., Ernst M., Meier B.H., Saupe S.J., and Riek R. Correlation of structural elements and infectivity of the HET-s prion. Nature 435 (2005) 844-848. The authors employ 2D ssNMR to determine the sequence-specific positions of amyloid fibril secondary structure elements of HET-s(218-289) fibrils. Structure-based mutagenesis reveals that the fibril conformation is the functional and infectious entity of the HET-s prion.
    • (2005) Nature , vol.435 , pp. 844-848
    • Ritter, C.1    Maddelein, M.-L.2    Siemer, A.B.3    Luhrs, T.4    Ernst, M.5    Meier, B.H.6    Saupe, S.J.7    Riek, R.8
  • 26
    • 1842637853 scopus 로고    scopus 로고
    • Absolute structural constraints on amyloid fibrils from solid-state NMR spectroscopy of partially oriented samples
    • Oyler N.A., and Tycko R. Absolute structural constraints on amyloid fibrils from solid-state NMR spectroscopy of partially oriented samples. J Am Chem Soc 126 (2004) 4478-4479
    • (2004) J Am Chem Soc , vol.126 , pp. 4478-4479
    • Oyler, N.A.1    Tycko, R.2
  • 27
    • 19944375100 scopus 로고    scopus 로고
    • Investigations of the structure and dynamics of membrane-associated peptides by magic angle spinning NMR
    • Huster D. Investigations of the structure and dynamics of membrane-associated peptides by magic angle spinning NMR. Prog Nucl Magn Reson Spectrosc 46 (2005) 79-107
    • (2005) Prog Nucl Magn Reson Spectrosc , vol.46 , pp. 79-107
    • Huster, D.1
  • 28
    • 4544369426 scopus 로고    scopus 로고
    • Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy
    • Giraud N., Böckmann A., Lesage A., Penin F., Blackledge M., and Emsley L. Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy. J Am Chem Soc 126 (2004) 11422-11423
    • (2004) J Am Chem Soc , vol.126 , pp. 11422-11423
    • Giraud, N.1    Böckmann, A.2    Lesage, A.3    Penin, F.4    Blackledge, M.5    Emsley, L.6
  • 31
    • 23844490048 scopus 로고    scopus 로고
    • Characterization of dynamics of perdeuterated proteins by MAS solid-state NMR
    • Hologne M., Faelber K., Diehl A., and Reif B. Characterization of dynamics of perdeuterated proteins by MAS solid-state NMR. J Am Chem Soc 127 (2005) 11208-11209
    • (2005) J Am Chem Soc , vol.127 , pp. 11208-11209
    • Hologne, M.1    Faelber, K.2    Diehl, A.3    Reif, B.4
  • 32
    • 25844493112 scopus 로고    scopus 로고
    • Capturing intermediate structures of Alzheimer's β-amyloid, Aβ(1-40), by solid-state NMR spectroscopy
    • Intermediate species in fibril formation for a 40-residue Alzheimer's β-amyloid peptide are investigated by a combination of fluorescence spectroscopy, electron microscopy and 2D ssNMR. In agreement with earlier studies, the results provide evidence that spherical amyloid intermediates of 15-30 nm in diameter exist before fibril formation of Aβ (1-40) fibrils and that these intermediates involve well-ordered β-sheets in the C-terminal and hydrophobic core regions.
    • Chimon S., and Ishii Y. Capturing intermediate structures of Alzheimer's β-amyloid, Aβ(1-40), by solid-state NMR spectroscopy. J Am Chem Soc 127 (2005) 13472-13473. Intermediate species in fibril formation for a 40-residue Alzheimer's β-amyloid peptide are investigated by a combination of fluorescence spectroscopy, electron microscopy and 2D ssNMR. In agreement with earlier studies, the results provide evidence that spherical amyloid intermediates of 15-30 nm in diameter exist before fibril formation of Aβ (1-40) fibrils and that these intermediates involve well-ordered β-sheets in the C-terminal and hydrophobic core regions.
    • (2005) J Am Chem Soc , vol.127 , pp. 13472-13473
    • Chimon, S.1    Ishii, Y.2
  • 33
    • 14744272629 scopus 로고    scopus 로고
    • Probing site-specific conformational distributions in protein folding with solid-state NMR
    • Havlin R.H., and Tycko R. Probing site-specific conformational distributions in protein folding with solid-state NMR. Proc Natl Acad Sci USA 102 (2005) 3284-3289
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3284-3289
    • Havlin, R.H.1    Tycko, R.2
  • 34
    • 24144475875 scopus 로고    scopus 로고
    • Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations
    • Heise H., Luca S., de Groot B.L., Grubmuller H., and Baldus M. Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations. Biophys J 89 (2005) 2113-2120
    • (2005) Biophys J , vol.89 , pp. 2113-2120
    • Heise, H.1    Luca, S.2    de Groot, B.L.3    Grubmuller, H.4    Baldus, M.5
  • 35
    • 0036289241 scopus 로고    scopus 로고
    • Novel NMR tools to study structure and dynamics of biomembranes
    • Gawrisch K., Eldho N.V., and Polozov I.V. Novel NMR tools to study structure and dynamics of biomembranes. Chem Phys Lipids 116 (2002) 135-151
    • (2002) Chem Phys Lipids , vol.116 , pp. 135-151
    • Gawrisch, K.1    Eldho, N.V.2    Polozov, I.V.3
  • 36
    • 25144453329 scopus 로고    scopus 로고
    • Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy
    • Andronesi O.C., Becker S., Seidel K., Heise H., Young H.S., and Baldus M. Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. J Am Chem Soc 127 (2005) 12965-12974
    • (2005) J Am Chem Soc , vol.127 , pp. 12965-12974
    • Andronesi, O.C.1    Becker, S.2    Seidel, K.3    Heise, H.4    Young, H.S.5    Baldus, M.6
  • 37
    • 28444473536 scopus 로고    scopus 로고
    • Simulation of fluorescence anisotropy experiments: probing protein dynamics
    • Schroder G.F., Alexiev U., and Grubmuller H. Simulation of fluorescence anisotropy experiments: probing protein dynamics. Biophys J 89 (2005) 3757-3770
    • (2005) Biophys J , vol.89 , pp. 3757-3770
    • Schroder, G.F.1    Alexiev, U.2    Grubmuller, H.3
  • 38
    • 0031201794 scopus 로고    scopus 로고
    • Selective homonuclear polarization transfer in the tilted rotating frame under magic angle spinning in solids
    • Takegoshi K., Nomura K., and Terao T. Selective homonuclear polarization transfer in the tilted rotating frame under magic angle spinning in solids. J Magn Reson 127 (1997) 206-216
    • (1997) J Magn Reson , vol.127 , pp. 206-216
    • Takegoshi, K.1    Nomura, K.2    Terao, T.3
  • 40
    • 0037151636 scopus 로고    scopus 로고
    • Structural constraints from proton-mediated rare-spin correlation spectroscopy in rotating solids
    • Lange A., Luca S., and Baldus M. Structural constraints from proton-mediated rare-spin correlation spectroscopy in rotating solids. J Am Chem Soc 124 (2002) 9704-9705
    • (2002) J Am Chem Soc , vol.124 , pp. 9704-9705
    • Lange, A.1    Luca, S.2    Baldus, M.3
  • 41
    • 8844247837 scopus 로고    scopus 로고
    • Probing molecular interfaces using 2D magic-angle-spinning NMR on protein mixtures with different uniform labeling
    • Etzkorn M., Böckmann A., Lange A., and Baldus M. Probing molecular interfaces using 2D magic-angle-spinning NMR on protein mixtures with different uniform labeling. J Am Chem Soc 126 (2004) 14746-14751
    • (2004) J Am Chem Soc , vol.126 , pp. 14746-14751
    • Etzkorn, M.1    Böckmann, A.2    Lange, A.3    Baldus, M.4
  • 42
    • 0038209242 scopus 로고    scopus 로고
    • Constraints on supramolecular structure in amyloid fibrils from two-dimensional solid-state NMR spectroscopy with uniform isotopic labeling
    • Tycko R., and Ishii Y. Constraints on supramolecular structure in amyloid fibrils from two-dimensional solid-state NMR spectroscopy with uniform isotopic labeling. J Am Chem Soc 125 (2003) 6606-6607
    • (2003) J Am Chem Soc , vol.125 , pp. 6606-6607
    • Tycko, R.1    Ishii, Y.2
  • 43
    • 26444593282 scopus 로고    scopus 로고
    • Intermolecular packing and alignment in an ordered β-hairpin antimicrobial peptide aggregate from 2D solid-state NMR
    • Tang M., Waring A.J., and Hong M. Intermolecular packing and alignment in an ordered β-hairpin antimicrobial peptide aggregate from 2D solid-state NMR. J Am Chem Soc 127 (2005) 13919-13927
    • (2005) J Am Chem Soc , vol.127 , pp. 13919-13927
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 45
    • 0037038365 scopus 로고    scopus 로고
    • Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
    • Castellani F., van Rossum B., Diehl A., Schubert M., Rehbein K., and Oschkinat H. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy. Nature 420 (2002) 98-102
    • (2002) Nature , vol.420 , pp. 98-102
    • Castellani, F.1    van Rossum, B.2    Diehl, A.3    Schubert, M.4    Rehbein, K.5    Oschkinat, H.6
  • 46
    • 17044380266 scopus 로고    scopus 로고
    • A concept for rapid protein-structure determination by solid-state NMR spectroscopy
    • Lange A., Becker S., Seidel K., Giller K., Pongs O., and Baldus M. A concept for rapid protein-structure determination by solid-state NMR spectroscopy. Angew Chem Int Ed Engl 44 (2005) 2089-2092
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 2089-2092
    • Lange, A.1    Becker, S.2    Seidel, K.3    Giller, K.4    Pongs, O.5    Baldus, M.6
  • 47
    • 20944434430 scopus 로고    scopus 로고
    • Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin
    • Zech S.G., Wand A.J., and McDermott A.E. Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin. J Am Chem Soc 127 (2005) 8618-8626
    • (2005) J Am Chem Soc , vol.127 , pp. 8618-8626
    • Zech, S.G.1    Wand, A.J.2    McDermott, A.E.3
  • 49
    • 0141988942 scopus 로고    scopus 로고
    • Analysis of proton-proton transfer dynamics in rotating solids and their use for 3D structure determination
    • Lange A., Seidel K., Verdier L., Luca S., and Baldus M. Analysis of proton-proton transfer dynamics in rotating solids and their use for 3D structure determination. J Am Chem Soc 125 (2003) 12640-12648
    • (2003) J Am Chem Soc , vol.125 , pp. 12640-12648
    • Lange, A.1    Seidel, K.2    Verdier, L.3    Luca, S.4    Baldus, M.5
  • 50
    • 21244479996 scopus 로고    scopus 로고
    • Powder crystallography by proton solid-state NMR spectroscopy
    • Elena B., and Emsley L. Powder crystallography by proton solid-state NMR spectroscopy. J Am Chem Soc 127 (2005) 9140-9146
    • (2005) J Am Chem Soc , vol.127 , pp. 9140-9146
    • Elena, B.1    Emsley, L.2
  • 51
    • 33645505791 scopus 로고    scopus 로고
    • Solid-State NMR Studies of the structure, dynamics, and assembly of β-sheet membrane peptides and α-helical membrane proteins with antibiotic activities
    • This review shows the versatility of state-of-the-art ssNMR to study structure, dynamics and assembly of β-sheet membrane peptides and α-helical membrane proteins with antibiotic activities.
    • Hong M. Solid-State NMR Studies of the structure, dynamics, and assembly of β-sheet membrane peptides and α-helical membrane proteins with antibiotic activities. Acc Chem Res 39 (2006) 176-183. This review shows the versatility of state-of-the-art ssNMR to study structure, dynamics and assembly of β-sheet membrane peptides and α-helical membrane proteins with antibiotic activities.
    • (2006) Acc Chem Res , vol.39 , pp. 176-183
    • Hong, M.1
  • 52
    • 33749066625 scopus 로고    scopus 로고
    • Etzkorn M, Matell S, Andronesi OC, Seidel K, Engelhard M, Baldus M: Secondary structure, dynamics and topology of a seven-helix receptor in native membranes studied by solid-state NMR. Angew Chem Int Ed Engl 2006, in press.
  • 53
    • 0242267593 scopus 로고    scopus 로고
    • 13C solid-state NMR spectroscopy
    • 13C solid-state NMR spectroscopy. J Am Chem Soc 125 (2003) 13336-13337
    • (2003) J Am Chem Soc , vol.125 , pp. 13336-13337
    • Lesage, A.1    Böckmann, A.2
  • 54
    • 23844547333 scopus 로고    scopus 로고
    • Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of α-spectrin by MAS solid-state NMR
    • Chevelkov V., Faelber K., Diehl A., Heinemann U., Oschkinat H., and Reif B. Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of α-spectrin by MAS solid-state NMR. J Biomol NMR 31 (2005) 295-310
    • (2005) J Biomol NMR , vol.31 , pp. 295-310
    • Chevelkov, V.1    Faelber, K.2    Diehl, A.3    Heinemann, U.4    Oschkinat, H.5    Reif, B.6
  • 55
    • 33645858263 scopus 로고    scopus 로고
    • Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR
    • 15N) constituents revealed that high-affinity binding of the toxin to the channel is associated with significant structural rearrangements in both molecules.
    • 15N) constituents revealed that high-affinity binding of the toxin to the channel is associated with significant structural rearrangements in both molecules.
    • (2006) Nature , vol.440 , pp. 959-962
    • Lange, A.1    Giller, K.2    Hornig, S.3    Martin-Eauclaire, M.-F.4    Pongs, O.5    Becker, S.6    Baldus, M.7
  • 57
    • 25844448515 scopus 로고    scopus 로고
    • SOLARIA: A protocol for automated cross-peak assignment and structure calculation for solid-state magic-angle spinning NMR spectroscopy
    • 13C) 2D ssNMR data in an automated manner. The described procedure leads to 20% more cross-peaks than in the previous manual assignment procedure and results in a 3D structure of a microcrystalline protein (1.3 Å rmsd to the X-ray reference) after a few hours.
    • 13C) 2D ssNMR data in an automated manner. The described procedure leads to 20% more cross-peaks than in the previous manual assignment procedure and results in a 3D structure of a microcrystalline protein (1.3 Å rmsd to the X-ray reference) after a few hours.
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 6151-6154
    • Fossi, M.1    Castellani, F.2    Nilges, M.3    Oschkinat, H.4    van Rossum, B.J.5


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