-
1
-
-
32344445231
-
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
-
2
-
-
0025729473
-
Determination of membrane-protein structure by rotational resonance NMR - Bacteriorhodopsin
-
Creuzet F., McDermott A., Gebhard R., Vanderhoef K., Spijkerassink M.B., Herzfeld J., Lugtenburg J., Levitt M.H., and Griffin R.G. Determination of membrane-protein structure by rotational resonance NMR - Bacteriorhodopsin. Science 251 (1991) 783-786
-
(1991)
Science
, vol.251
, pp. 783-786
-
-
Creuzet, F.1
McDermott, A.2
Gebhard, R.3
Vanderhoef, K.4
Spijkerassink, M.B.5
Herzfeld, J.6
Lugtenburg, J.7
Levitt, M.H.8
Griffin, R.G.9
-
4
-
-
0037195278
-
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
-
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
-
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
-
7
-
-
33744804804
-
Homonuclear and heteronuclear NMR studies of a statherin fragment bound to hydroxyapatite crystals
-
Raghunathan V., Gibson J.M., Goobes G., Popham J.M., Louie E.A., Stayton P.S., and Drobny G.P. Homonuclear and heteronuclear NMR studies of a statherin fragment bound to hydroxyapatite crystals. J Phys Chem B Condens Matter Mater Surf Interfaces Biophys 110 (2006) 9324-9332
-
(2006)
J Phys Chem B Condens Matter Mater Surf Interfaces Biophys
, vol.110
, pp. 9324-9332
-
-
Raghunathan, V.1
Gibson, J.M.2
Goobes, G.3
Popham, J.M.4
Louie, E.A.5
Stayton, P.S.6
Drobny, G.P.7
-
8
-
-
2342482988
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
16
-
-
0141703292
-
The conformation of neurotensin bound to its G protein-coupled receptor
-
Luca S., White J.F., Sohal A.K., Filippov D.V., van Boom J.H., Grisshammer R., and Baldus M. The conformation of neurotensin bound to its G protein-coupled receptor. Proc Natl Acad Sci USA 100 (2003) 10706-10711
-
(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 10706-10711
-
-
Luca, S.1
White, J.F.2
Sohal, A.K.3
Filippov, D.V.4
van Boom, J.H.5
Grisshammer, R.6
Baldus, M.7
-
17
-
-
1942532326
-
Towards structure determination of neurotoxin II bound to nicotinic acetylcholine receptor: a solid-state NMR approach
-
Krabben L., van Rossum B.J., Castellani F., Bocharov E., Schulga A.A., Arseniev A.S., Weise C., Hucho F., and Oschkinata H. Towards structure determination of neurotoxin II bound to nicotinic acetylcholine receptor: a solid-state NMR approach. FEBS Lett 564 (2004) 319-324
-
(2004)
FEBS Lett
, vol.564
, pp. 319-324
-
-
Krabben, L.1
van Rossum, B.J.2
Castellani, F.3
Bocharov, E.4
Schulga, A.A.5
Arseniev, A.S.6
Weise, C.7
Hucho, F.8
Oschkinata, H.9
-
18
-
-
33644613761
-
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
-
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
-
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
-
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
-
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
-
25
-
-
19944428721
-
Probing membrane protein structure and orientation under fast magic-angle-spinning
-
Andronesi O.C., Pfeifer J.R., Al-Momani L., Özdirekcan S., Rijkers D.T.S., Angerstein B., Luca S., Koert U., Killian J.A., and Baldus M. Probing membrane protein structure and orientation under fast magic-angle-spinning. J Biomol NMR 30 (2004) 253-265
-
(2004)
J Biomol NMR
, vol.30
, pp. 253-265
-
-
Andronesi, O.C.1
Pfeifer, J.R.2
Al-Momani, L.3
Özdirekcan, S.4
Rijkers, D.T.S.5
Angerstein, B.6
Luca, S.7
Koert, U.8
Killian, J.A.9
Baldus, M.10
-
26
-
-
1842637853
-
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
-
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
-
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
-
29
-
-
24644462659
-
13C chemical shift assignments and conformational analysis
-
13C chemical shift assignments and conformational analysis. J Am Chem Soc 127 (2005) 12291-12305
-
(2005)
J Am Chem Soc
, vol.127
, pp. 12291-12305
-
-
Franks, W.T.1
Zhou, D.H.2
Wylie, B.J.3
Money, B.G.4
Graesser, D.T.5
Frericks, H.L.6
Sahota, G.7
Rienstra, C.M.8
-
31
-
-
23844490048
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
44
-
-
33745141876
-
13C dipolar correlations: coexistence of dimer-based and pseudo-monomer-based stackings
-
13C dipolar correlations: coexistence of dimer-based and pseudo-monomer-based stackings. Biochemistry 45 (2006) 7574-7585
-
(2006)
Biochemistry
, vol.45
, pp. 7574-7585
-
-
Kakitani, Y.1
Nagae, H.2
Mizoguchi, T.3
Egawa, A.4
Akiba, K.5
Fujiwara, T.6
Akutsu, H.7
Koyama, Y.8
-
45
-
-
0037038365
-
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
-
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
-
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
-
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
-
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
-
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
-
-
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
-
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
-
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
-
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
-
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
|