-
1
-
-
0032986388
-
Solid-state nuclear magnetic resonance investigation of protein and polypeptide structure
-
Fu R., Cross T.A. Solid-state nuclear magnetic resonance investigation of protein and polypeptide structure. Annu Rev Biophys Biomol Struct. 28:1999;235-268.
-
(1999)
Annu Rev Biophys Biomol Struct
, vol.28
, pp. 235-268
-
-
Fu, R.1
Cross, T.A.2
-
2
-
-
0027360175
-
High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
-
Ketchem R.R., Hu W., Cross T.A. High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science. 261:1993;1457-1460.
-
(1993)
Science
, vol.261
, pp. 1457-1460
-
-
Ketchem, R.R.1
Hu, W.2
Cross, T.A.3
-
3
-
-
0032919444
-
Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
-
Opella S.J., Marassi F.M., Gesell J.J., Valente A.P., Kim Y., Oblatt-Montal M., Montal M. Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat Struct Biol. 6:1999;374-379.
-
(1999)
Nat Struct Biol
, vol.6
, pp. 374-379
-
-
Opella, S.J.1
Marassi, F.M.2
Gesell, J.J.3
Valente, A.P.4
Kim, Y.5
Oblatt-Montal, M.6
Montal, M.7
-
5
-
-
0034743151
-
Biomolecular solid state NMR: Advances in structural methodology and applications to peptide and protein fibrils
-
Tycko R. Biomolecular solid state NMR: advances in structural methodology and applications to peptide and protein fibrils. Annu Rev Phys Chem. 52:2001;575-606.
-
(2001)
Annu Rev Phys Chem
, vol.52
, pp. 575-606
-
-
Tycko, R.1
-
6
-
-
0031853671
-
Dipolar recoupling in MAS spectra of biological solids
-
Griffin R.G. Dipolar recoupling in MAS spectra of biological solids. Nat Struct Biol Suppl. 5:1998;508-512.
-
(1998)
Nat Struct Biol Suppl
, vol.5
, pp. 508-512
-
-
Griffin, R.G.1
-
7
-
-
0035795429
-
15N signal assignments of the α-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla
-
This paper demonstrates an important step in the structure determination of uniformly labeled solid proteins - the sequential assignment. Nearly all of the carbon and nitrogen resonances of microcrystalline samples of the SH3 domain are assigned through homonuclear and heteronuclear dipolar correlations in spectra from two-dimensional magic-angle spinning NMR.
-
15N signal assignments of the α-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla. Chembiochem. 2:2001;272-281. This paper demonstrates an important step in the structure determination of uniformly labeled solid proteins - the sequential assignment. Nearly all of the carbon and nitrogen resonances of microcrystalline samples of the SH3 domain are assigned through homonuclear and heteronuclear dipolar correlations in spectra from two-dimensional magic-angle spinning NMR.
-
(2001)
Chembiochem
, vol.2
, pp. 272-281
-
-
Pauli, J.1
Baldus, M.2
Van Rossum, B.3
De Groot, H.4
Oschkinat, H.5
-
9
-
-
0034167578
-
Sample optimization and identification of signal patterns of amino acid side chains in 2D RFDR spectra of the α-spectrin SH3 domain
-
Pauli J., van Rossum B., Forster H., de Groot H.J., Oschkinat H. Sample optimization and identification of signal patterns of amino acid side chains in 2D RFDR spectra of the α-spectrin SH3 domain. J Magn Reson. 143:2000;411-416.
-
(2000)
J Magn Reson
, vol.143
, pp. 411-416
-
-
Pauli, J.1
Van Rossum, B.2
Forster, H.3
De Groot, H.J.4
Oschkinat, H.5
-
10
-
-
0035072686
-
15N] labeled membrane-protein complex at ultra-high magnetic fields
-
15N] labeled membrane-protein complex at ultra-high magnetic fields. J Biomol NMR. 19:2001;243-253.
-
(2001)
J Biomol NMR
, vol.19
, pp. 243-253
-
-
Egorova-Zachernyuk, T.A.1
Hollander, J.2
Fraser, N.3
Gast, P.4
Hoff, A.J.5
Cogdell, R.6
De Groot, H.J.7
Baldus, M.8
-
11
-
-
0034846331
-
Secondary chemical shifts in immobilized peptides and proteins: A qualitative basis for structure refinement under magic angle spinning
-
Luca S., Filippov D.V., van Boom J.H., Oschkinat H., de Groot H.J., Baldus M. Secondary chemical shifts in immobilized peptides and proteins: a qualitative basis for structure refinement under magic angle spinning. J Biomol NMR. 20:2001;325-331.
-
(2001)
J Biomol NMR
, vol.20
, pp. 325-331
-
-
Luca, S.1
Filippov, D.V.2
Van Boom, J.H.3
Oschkinat, H.4
De Groot, H.J.5
Baldus, M.6
-
12
-
-
0035872678
-
13C dipolar coupling under very fast magic angle spinning in solid-state nuclear magnetic resonance: Applications to distance measurements, spectral assignments, and high-throughput secondary structure determination
-
13C dipolar coupling under very fast magic angle spinning in solid-state nuclear magnetic resonance: applications to distance measurements, spectral assignments, and high-throughput secondary structure determination. J Chem Phys. 114:2001;8473-8483.
-
(2001)
J Chem Phys
, vol.114
, pp. 8473-8483
-
-
Ishii, Y.1
-
15
-
-
45149145322
-
Rotational-echo double-resonance NMR
-
Gullion T., Schaefer J. Rotational-echo double-resonance NMR. J Magn Reson. 81:1989;196-200.
-
(1989)
J Magn Reson
, vol.81
, pp. 196-200
-
-
Gullion, T.1
Schaefer, J.2
-
16
-
-
0035956534
-
15N-labeled membrane protein: Distances between the Schiff base and aspartic acids in the active site of bacteriorhodopsin
-
This application of the new frequency-selective REDOR experiment to bacteriorhodopsin shows the promise of this method for mapping multiple distances in the active site of a uniformly labeled membrane protein. Distances in the 4-5 Å range are measured from the Schiff base nitrogen to two important aspartate carboxyls.
-
15N-labeled membrane protein: distances between the Schiff base and aspartic acids in the active site of bacteriorhodopsin. J Am Chem Soc. 123:2001;12929-12930. This application of the new frequency-selective REDOR experiment to bacteriorhodopsin shows the promise of this method for mapping multiple distances in the active site of a uniformly labeled membrane protein. Distances in the 4-5 Å range are measured from the Schiff base nitrogen to two important aspartate carboxyls.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 12929-12930
-
-
Jaroniec, C.P.1
Lansing, J.C.2
Tounge, B.A.3
Belenky, M.4
Herzfeld, J.5
Griffin, R.G.6
-
17
-
-
0034610393
-
Structural insights into the binding of cardiac glycosides to the digitalis receptor revealed by solid-state NMR
-
Middleton D.A., Rankin S., Esmann M., Watts A. Structural insights into the binding of cardiac glycosides to the digitalis receptor revealed by solid-state NMR. Proc Natl Acad Sci USA. 97:2000;13602-13607.
-
(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 13602-13607
-
-
Middleton, D.A.1
Rankin, S.2
Esmann, M.3
Watts, A.4
-
19
-
-
0037133147
-
Tryptophan interactions in bacteriorhodopsin: A heteronuclear solid-state NMR study
-
Petkova A.T., Hatanaka M., Jaroniec C.P., Hu J.G., Belenky M., Verhoeven M., Lugtenburg J., Griffin R.G., Herzfeld J. Tryptophan interactions in bacteriorhodopsin: a heteronuclear solid-state NMR study. Biochemistry. 41:2002;2429-2437.
-
(2002)
Biochemistry
, vol.41
, pp. 2429-2437
-
-
Petkova, A.T.1
Hatanaka, M.2
Jaroniec, C.P.3
Hu, J.G.4
Belenky, M.5
Verhoeven, M.6
Lugtenburg, J.7
Griffin, R.G.8
Herzfeld, J.9
-
21
-
-
0034763782
-
Solid-state NMR structure determination of melittin in a lipid environment
-
Lam Y.H., Wassall S.R., Morton C.J., Smith R., Separovic F. Solid-state NMR structure determination of melittin in a lipid environment. Biophys J. 81:2001;2752-2761.
-
(2001)
Biophys J
, vol.81
, pp. 2752-2761
-
-
Lam, Y.H.1
Wassall, S.R.2
Morton, C.J.3
Smith, R.4
Separovic, F.5
-
22
-
-
0035834520
-
Helical structure of phospholamban in membrane bilayers
-
Smith S.O., Kawakami T., Liu W., Ziliox M., Aimoto S. Helical structure of phospholamban in membrane bilayers. J Mol Biol. 313:2001;1139-1148.
-
(2001)
J Mol Biol
, vol.313
, pp. 1139-1148
-
-
Smith, S.O.1
Kawakami, T.2
Liu, W.3
Ziliox, M.4
Aimoto, S.5
-
23
-
-
0035838516
-
Solid-state nuclear magnetic resonance evidence for an extended β strand conformation of the membrane-bound HIV-1 fusion peptide
-
Yang J., Gabrys C.M., Weliky D.P. Solid-state nuclear magnetic resonance evidence for an extended β strand conformation of the membrane-bound HIV-1 fusion peptide. Biochemistry. 40:2001;8126-8137.
-
(2001)
Biochemistry
, vol.40
, pp. 8126-8137
-
-
Yang, J.1
Gabrys, C.M.2
Weliky, D.P.3
-
24
-
-
0036224950
-
Implications of threonine hydrogen bonding in the glycophorin A transmembrane helix dimer
-
Smith S.O., Eilers M., Song D., Crocker E., Ying W., Groesbeek M., Metz G., Ziliox M., Aimoto S. Implications of threonine hydrogen bonding in the glycophorin A transmembrane helix dimer. Biophys J. 82:2002;2476-2486.
-
(2002)
Biophys J
, vol.82
, pp. 2476-2486
-
-
Smith, S.O.1
Eilers, M.2
Song, D.3
Crocker, E.4
Ying, W.5
Groesbeek, M.6
Metz, G.7
Ziliox, M.8
Aimoto, S.9
-
25
-
-
0034700129
-
Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils
-
Antzutkin O.N., Balbach J.J., Leapman R.D., Rizzo N.W., Reed J., Tycko R. Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils. Proc Natl Acad Sci USA. 97:2000;13045-13050.
-
(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 13045-13050
-
-
Antzutkin, O.N.1
Balbach, J.J.2
Leapman, R.D.3
Rizzo, N.W.4
Reed, J.5
Tycko, R.6
-
26
-
-
0037066607
-
Conformational changes of colicin Ia channel-forming domain upon membrane binding: A solid-state NMR study
-
Huster D., Yao X., Jakes K., Hong M. Conformational changes of colicin Ia channel-forming domain upon membrane binding: a solid-state NMR study. Biochim Biophys Acta. 1561:2002;159-170.
-
(2002)
Biochim Biophys Acta
, vol.1561
, pp. 159-170
-
-
Huster, D.1
Yao, X.2
Jakes, K.3
Hong, M.4
-
27
-
-
0035954376
-
Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain
-
Measurements of dynamics of the pore-forming colicin Ia protein in the aqueous and membrane-bound states of this protein show increased mobility on membrane binding, which is consistent with current views of this protein. This study highlights the many different solid-state NMR experiments that can probe a variety of motional timescales and that, when combined with an extensive labeling protocol, can probe global dynamics throughout the protein.
-
Huster D., Xiao L., Hong M. Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain. Biochemistry. 40:2001;7662-7674. Measurements of dynamics of the pore-forming colicin Ia protein in the aqueous and membrane-bound states of this protein show increased mobility on membrane binding, which is consistent with current views of this protein. This study highlights the many different solid-state NMR experiments that can probe a variety of motional timescales and that, when combined with an extensive labeling protocol, can probe global dynamics throughout the protein.
-
(2001)
Biochemistry
, vol.40
, pp. 7662-7674
-
-
Huster, D.1
Xiao, L.2
Hong, M.3
-
28
-
-
0034685511
-
Solid-state NMR determination of 13Cα chemical shift anisotropies for the identification of protein secondary structure
-
Hong M. Solid-state NMR determination of 13Cα chemical shift anisotropies for the identification of protein secondary structure. J Am Chem Soc. 122:2000;3762-3770.
-
(2000)
J Am Chem Soc
, vol.122
, pp. 3762-3770
-
-
Hong, M.1
-
29
-
-
0034703698
-
Efficient β-sheet identification in proteins by solid-state NMR spectroscopy
-
Huster D., Yamaguchi S., Hong M. Efficient β-sheet identification in proteins by solid-state NMR spectroscopy. J Am Chem Soc. 122:2000;11320-11327.
-
(2000)
J Am Chem Soc
, vol.122
, pp. 11320-11327
-
-
Huster, D.1
Yamaguchi, S.2
Hong, M.3
-
30
-
-
0035798396
-
Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form
-
For studies of biosynthetically labeled large proteins, methods are needed to direct the experiment to the site of interest in a background of other labeled sites. This paper describes a novel NMR approach: sequential labeling of residues that occur as unique dipeptides in the sequence of the 13 kDa HIV-1 Rev protein and double quantum NMR methods are used to measure structural constraints determining the backbone conformation at several sites.
-
Blanco F.J., Hess S., Pannell L.K., Rizzo N.W., Tycko R. Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form. J Mol Biol. 313:2001;845-859. For studies of biosynthetically labeled large proteins, methods are needed to direct the experiment to the site of interest in a background of other labeled sites. This paper describes a novel NMR approach: sequential labeling of residues that occur as unique dipeptides in the sequence of the 13 kDa HIV-1 Rev protein and double quantum NMR methods are used to measure structural constraints determining the backbone conformation at several sites.
-
(2001)
J Mol Biol
, vol.313
, pp. 845-859
-
-
Blanco, F.J.1
Hess, S.2
Pannell, L.K.3
Rizzo, N.W.4
Tycko, R.5
-
31
-
-
0037022825
-
Site-directed rotational resonance solid-state NMR distance measurements probe structure and mechanism in the transmembrane domain of the serine bacterial chemoreceptor
-
This study uses a biochemical approach to direct the NMR experiment to a specific site in the 60 kDa membrane-bound Ser receptor: site-directed mutagenesis introduces a unique residue for distance measurements that test current models for both the structure of the transmembrane domain and for the ligand-induced conformational change. A subtraction method for correcting for natural abundance contributions is demonstrated in this first application of rotational resonance to measure a distance involving an unresolved resonance.
-
Isaac B., Gallagher G.J., Balazs Y.S., Thompson L.K. Site-directed rotational resonance solid-state NMR distance measurements probe structure and mechanism in the transmembrane domain of the serine bacterial chemoreceptor. Biochemistry. 41:2002;3025-3036. This study uses a biochemical approach to direct the NMR experiment to a specific site in the 60 kDa membrane-bound Ser receptor: site-directed mutagenesis introduces a unique residue for distance measurements that test current models for both the structure of the transmembrane domain and for the ligand-induced conformational change. A subtraction method for correcting for natural abundance contributions is demonstrated in this first application of rotational resonance to measure a distance involving an unresolved resonance.
-
(2002)
Biochemistry
, vol.41
, pp. 3025-3036
-
-
Isaac, B.1
Gallagher, G.J.2
Balazs, Y.S.3
Thompson, L.K.4
-
32
-
-
0036176305
-
Measurement of conformational constraints in an elastin-mimetic protein by residue-pair selected solid-state NMR
-
Hong M., McMillan R.A., Conticello V.P. Measurement of conformational constraints in an elastin-mimetic protein by residue-pair selected solid-state NMR. J Biomol NMR. 22:2002;175-179.
-
(2002)
J Biomol NMR
, vol.22
, pp. 175-179
-
-
Hong, M.1
McMillan, R.A.2
Conticello, V.P.3
-
33
-
-
0035814825
-
Site-directed solid-state NMR measurement of a ligand-induced conformational change in the serine bacterial chemoreceptor
-
Interhelical distance measurements in two signaling states provide the first high-resolution measurement of the ligand-induced conformational change in an intact, membrane-bound chemotaxis receptor. Such experiments can map and follow this change to determine the mechanism in the native protein.
-
Murphy O.J. III, Kovacs F.A., Sicard E.L., Thompson L.K. Site-directed solid-state NMR measurement of a ligand-induced conformational change in the serine bacterial chemoreceptor. Biochemistry. 40:2001;1358-1366. Interhelical distance measurements in two signaling states provide the first high-resolution measurement of the ligand-induced conformational change in an intact, membrane-bound chemotaxis receptor. Such experiments can map and follow this change to determine the mechanism in the native protein.
-
(2001)
Biochemistry
, vol.40
, pp. 1358-1366
-
-
Murphy O.J. III1
Kovacs, F.A.2
Sicard, E.L.3
Thompson, L.K.4
-
34
-
-
57249114947
-
The effect of RF inhomogeneity on heteronuclear dipolar recoupling in solid state NMR: Practical performance of SFAM and REDOR
-
Nishimura K., Fu R., Cross T.A. The effect of RF inhomogeneity on heteronuclear dipolar recoupling in solid state NMR: practical performance of SFAM and REDOR. J Magn Reson. 152:2001;227-233.
-
(2001)
J Magn Reson
, vol.152
, pp. 227-233
-
-
Nishimura, K.1
Fu, R.2
Cross, T.A.3
-
35
-
-
0031552562
-
Recoupling of heteronuclear dipolar interactions in solid state magic-angle spinning NMR by simultaneous frequency and amplitude modulation
-
Fu R.Q., Smith S.A., Bodenhausen G. Recoupling of heteronuclear dipolar interactions in solid state magic-angle spinning NMR by simultaneous frequency and amplitude modulation. Chem Phys Lett. 272:1997;361-369.
-
(1997)
Chem Phys Lett
, vol.272
, pp. 361-369
-
-
Fu, R.Q.1
Smith, S.A.2
Bodenhausen, G.3
-
36
-
-
0034571935
-
SIMPSON: A general simulation program for solid-state NMR spectroscopy
-
Bak M., Rasmussen J.T., Nielsen N.C. SIMPSON: a general simulation program for solid-state NMR spectroscopy. J Magn Reson. 147:2000;296-330.
-
(2000)
J Magn Reson
, vol.147
, pp. 296-330
-
-
Bak, M.1
Rasmussen, J.T.2
Nielsen, N.C.3
-
37
-
-
0035742331
-
Measurement of interfluorine distances in solids
-
Gilchrist M.L. Jr, Monde K., Tomita Y., Iwashita T., Nakanishi K., McDermott A.E. Measurement of interfluorine distances in solids. J Magn Reson. 152:2001;1-6.
-
(2001)
J Magn Reson
, vol.152
, pp. 1-6
-
-
Gilchrist M.L., Jr.1
Monde, K.2
Tomita, Y.3
Iwashita, T.4
Nakanishi, K.5
McDermott, A.E.6
-
39
-
-
0037138669
-
Bilayer sample for fast or slow magic angle oriented sample spinning solid-state NMR spectroscopy
-
Sizun C., Bechinger B. Bilayer sample for fast or slow magic angle oriented sample spinning solid-state NMR spectroscopy. J Am Chem Soc. 124:2002;1146-1147.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 1146-1147
-
-
Sizun, C.1
Bechinger, B.2
-
40
-
-
0034000232
-
Inter- and intramolecular distance measurements by solid-state MAS NMR: Determination of gramicidin A channel dimer structure in hydrated phospholipid bilayers
-
Fu R., Cotten M., Cross T.A. Inter- and intramolecular distance measurements by solid-state MAS NMR: determination of gramicidin A channel dimer structure in hydrated phospholipid bilayers. J Biomol NMR. 16:2000;261-268.
-
(2000)
J Biomol NMR
, vol.16
, pp. 261-268
-
-
Fu, R.1
Cotten, M.2
Cross, T.A.3
-
41
-
-
0037027306
-
+ channel helical bundle combining precise orientational and distance restraints from solid state NMR
-
in press
-
+ channel helical bundle combining precise orientational and distance restraints from solid state NMR. Biochemistry 2002, in press.
-
(2002)
Biochemistry
-
-
Nishimura, K.1
Kim, S.2
Zhang, L.3
Cross, T.A.4
-
42
-
-
0035811042
-
Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers
-
Smith S.O., Song D., Shekar S., Groesbeek M., Ziliox M., Aimoto S. Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers. Biochemistry. 40:2001;6553-6558.
-
(2001)
Biochemistry
, vol.40
, pp. 6553-6558
-
-
Smith, S.O.1
Song, D.2
Shekar, S.3
Groesbeek, M.4
Ziliox, M.5
Aimoto, S.6
-
43
-
-
0034649352
-
16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR
-
16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR. Biochemistry. 39:2000;13748-13759.
-
(2000)
Biochemistry
, vol.39
, pp. 13748-13759
-
-
Balbach, J.J.1
Ishii, Y.2
Antzutkin, O.N.3
Leapman, R.D.4
Rizzo, N.W.5
Dyda, F.6
Reed, J.7
Tycko, R.8
-
44
-
-
0035997080
-
Supramolecular structure in full-length Alzheimer's β-amyloid fibrils: Evidence for a parallel β-sheet organization from solid state NMR
-
Balbach J.J., Petkova A.T., Oyler N.A., Antzutkin O.N., Gordon D.J., Meredith S.C., Tycko R. Supramolecular structure in full-length Alzheimer's β-amyloid fibrils: evidence for a parallel β-sheet organization from solid state NMR. Biophys J. 83:2002;1205-1216.
-
(2002)
Biophys J
, vol.83
, pp. 1205-1216
-
-
Balbach, J.J.1
Petkova, A.T.2
Oyler, N.A.3
Antzutkin, O.N.4
Gordon, D.J.5
Meredith, S.C.6
Tycko, R.7
-
45
-
-
0034054969
-
Determination of statherin N-terminal peptide conformation on hydroxyapatite crystals
-
Shaw W.J., Long J.R., Dindot J.L., Campbell A.A., Stayton P.S., Drobny G.P. Determination of statherin N-terminal peptide conformation on hydroxyapatite crystals. J Am Chem Soc. 122:2000;1709-1716.
-
(2000)
J Am Chem Soc
, vol.122
, pp. 1709-1716
-
-
Shaw, W.J.1
Long, J.R.2
Dindot, J.L.3
Campbell, A.A.4
Stayton, P.S.5
Drobny, G.P.6
-
46
-
-
0034718060
-
A solid state NMR study of dynamics in a hydrated salivary peptide adsorbed to hydroxyapatite
-
Shaw W.J., Long J.R., Campbell A.A., Stayton P.S., Drobny G.P. A solid state NMR study of dynamics in a hydrated salivary peptide adsorbed to hydroxyapatite. J Am Chem Soc. 122:2000;7118-7119.
-
(2000)
J Am Chem Soc
, vol.122
, pp. 7118-7119
-
-
Shaw, W.J.1
Long, J.R.2
Campbell, A.A.3
Stayton, P.S.4
Drobny, G.P.5
-
47
-
-
0035951086
-
Structure and dynamics of hydrated statherin on hydroxyapatite as determined by solid-state NMR
-
Complementary information from various measurements of structure and dynamics on a peptide involved in biomineralization is combined to develop a model for the structure and surface interaction of the peptide.
-
Long J.R., Shaw W.J., Stayton P.S., Drobny G.P. Structure and dynamics of hydrated statherin on hydroxyapatite as determined by solid-state NMR. Biochemistry. 40:2001;15451-15455. Complementary information from various measurements of structure and dynamics on a peptide involved in biomineralization is combined to develop a model for the structure and surface interaction of the peptide.
-
(2001)
Biochemistry
, vol.40
, pp. 15451-15455
-
-
Long, J.R.1
Shaw, W.J.2
Stayton, P.S.3
Drobny, G.P.4
-
48
-
-
0037024166
-
Assembly of α-helical peptide coatings on hydrophobic surfaces
-
Long J.R., Oyler N., Drobny G.P., Stayton P.S. Assembly of α-helical peptide coatings on hydrophobic surfaces. J Am Chem Soc. 124:2002;6297-6303.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 6297-6303
-
-
Long, J.R.1
Oyler, N.2
Drobny, G.P.3
Stayton, P.S.4
-
49
-
-
0034717124
-
Chimeric peptides of statherin and osteopontin that bind hydroxyapatite and mediate cell adhesion
-
Gilbert M., Shaw W.J., Long J.R., Nelson K., Drobny G.P., Giachelli C.M., Stayton P.S. Chimeric peptides of statherin and osteopontin that bind hydroxyapatite and mediate cell adhesion. J Biol Chem. 275:2000;16213-16218.
-
(2000)
J Biol Chem
, vol.275
, pp. 16213-16218
-
-
Gilbert, M.1
Shaw, W.J.2
Long, J.R.3
Nelson, K.4
Drobny, G.P.5
Giachelli, C.M.6
Stayton, P.S.7
-
50
-
-
0037018918
-
Rotational-echo double resonance characterization of vancomycin binding sites in staphylococcus aureus
-
A model is developed for the binding site of a vancomycin derivative to the peptidoglycan of whole cells on the basis of various REDOR measurements in this extremely complex sample.
-
Kim S.J., Cegelski L., Studelska D.R., O'Connor R.D., Mehta A.K., Schaefer J. Rotational-echo double resonance characterization of vancomycin binding sites in staphylococcus aureus. Biochemistry. 41:2002;6967-6977. A model is developed for the binding site of a vancomycin derivative to the peptidoglycan of whole cells on the basis of various REDOR measurements in this extremely complex sample.
-
(2002)
Biochemistry
, vol.41
, pp. 6967-6977
-
-
Kim, S.J.1
Cegelski, L.2
Studelska, D.R.3
O'Connor, R.D.4
Mehta, A.K.5
Schaefer, J.6
-
51
-
-
0036298954
-
Relative CSA-dipolar orientation from REDOR sidebands
-
This variation of the REDOR method for heteronuclear dipolar coupling measurements could provide additional structural information in many REDOR studies. By simply using slower magic-angle spinning speeds and measuring the sideband intensities on the same sample, this experiment can measure the relative orientations of the dipolar and chemical shift anisotropy tensors.
-
O'Connor R.D., Schaefer J. Relative CSA-dipolar orientation from REDOR sidebands. J Magn Reson. 154:2002;46-52. This variation of the REDOR method for heteronuclear dipolar coupling measurements could provide additional structural information in many REDOR studies. By simply using slower magic-angle spinning speeds and measuring the sideband intensities on the same sample, this experiment can measure the relative orientations of the dipolar and chemical shift anisotropy tensors.
-
(2002)
J Magn Reson
, vol.154
, pp. 46-52
-
-
O'Connor, R.D.1
Schaefer, J.2
-
52
-
-
0034610347
-
Structural and mechanistic investigation of 3-deoxy-D-manno-octulosonate-8-phosphate synthase by solid-state REDOR NMR
-
Kaustov L., Kababya S., Du S., Baasov T., Gropper S., Shoham Y., Schmidt A. Structural and mechanistic investigation of 3-deoxy-D-manno-octulosonate-8-phosphate synthase by solid-state REDOR NMR. Biochemistry. 39:2000;14865-14876.
-
(2000)
Biochemistry
, vol.39
, pp. 14865-14876
-
-
Kaustov, L.1
Kababya, S.2
Du, S.3
Baasov, T.4
Gropper, S.5
Shoham, Y.6
Schmidt, A.7
-
53
-
-
0037023450
-
19F} REDOR NMR
-
19F} REDOR NMR. J Org Chem. 67:2002;2087-2092.
-
(2002)
J Org Chem
, vol.67
, pp. 2087-2092
-
-
Mehta, A.K.1
Studelska, D.R.2
Fischer, M.3
Giessauf, A.4
Kemter, K.5
Bacher, A.6
Cushman, M.7
Schaefer, J.8
-
54
-
-
0036158538
-
Control of the pump cycle in bacteriorhodopsin: Mechanisms elucidated by solid-state NMR of the D85N mutant
-
Hatcher M.E., Hu J.G., Belenky M., Verdegem P., Lugtenburg J., Griffin R.G., Herzfeld J. Control of the pump cycle in bacteriorhodopsin: mechanisms elucidated by solid-state NMR of the D85N mutant. Biophys J. 82:2002;1017-1029.
-
(2002)
Biophys J
, vol.82
, pp. 1017-1029
-
-
Hatcher, M.E.1
Hu, J.G.2
Belenky, M.3
Verdegem, P.4
Lugtenburg, J.5
Griffin, R.G.6
Herzfeld, J.7
-
55
-
-
0037080338
-
Chromophore distortions in the bacteriorhodopsin photocycle: Evolution of the H-C14-C15-H dihedral angle measured by solid-state NMR
-
Lansing J.C., Hohwy M., Jaroniec C.P., Creemers A.F., Lugtenburg J., Herzfeld J., Griffin R.G. Chromophore distortions in the bacteriorhodopsin photocycle: evolution of the H-C14-C15-H dihedral angle measured by solid-state NMR. Biochemistry. 41:2002;431-438.
-
(2002)
Biochemistry
, vol.41
, pp. 431-438
-
-
Lansing, J.C.1
Hohwy, M.2
Jaroniec, C.P.3
Creemers, A.F.4
Lugtenburg, J.5
Herzfeld, J.6
Griffin, R.G.7
-
56
-
-
0034100363
-
Determination of a molecular torsional angle in the metarhodopsin-I photointermediate of rhodopsin by double-quantum solid-state NMR
-
Feng X., Verdegem P.J., Eden M., Sandstrom D., Lee Y.K., Bovee-Geurts P.H., de Grip W.J., Lugtenburg J., de Groot H.J., Levitt M.H. Determination of a molecular torsional angle in the metarhodopsin-I photointermediate of rhodopsin by double-quantum solid-state NMR. J Biomol NMR. 16:2000;1-8.
-
(2000)
J Biomol NMR
, vol.16
, pp. 1-8
-
-
Feng, X.1
Verdegem, P.J.2
Eden, M.3
Sandstrom, D.4
Lee, Y.K.5
Bovee-Geurts, P.H.6
De Grip, W.J.7
Lugtenburg, J.8
De Groot, H.J.9
Levitt, M.H.10
-
57
-
-
0034924188
-
Segmental isotopic labeling using expressed protein ligation
-
Cowburn D., Muir T.W. Segmental isotopic labeling using expressed protein ligation. Methods Enzymol. 339:2001;41-54.
-
(2001)
Methods Enzymol
, vol.339
, pp. 41-54
-
-
Cowburn, D.1
Muir, T.W.2
-
58
-
-
0029865503
-
Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
-
Chervitz S.A., Falke J.J. Molecular mechanism of transmembrane signaling by the aspartate receptor: a model. Proc Natl Acad Sci USA. 93:1996;2545-2550.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 2545-2550
-
-
Chervitz, S.A.1
Falke, J.J.2
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