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Papers by Lynne Batchelder
Journal of magnetic resonance, Feb 1, 1980
The quadrupole coupling parameters for i4N in the two chemically inequivalent sites in paraelectr... more The quadrupole coupling parameters for i4N in the two chemically inequivalent sites in paraelectric ammonium sulfate have been measured by proton-nitrogen double resonance for the interval 225 K 5 TZ 365 K. Transition frequencies are represented to within ca. 0.2 kHz in this interval by Y+ (1)=242.43-0.33807; V-(I) = 144.03-0.1855 T; V+ (II) = 147.08-0.1294 T; V-(II) = 73.39-0.0281 T kHz, where T is the temperature in degrees Kelvin. These data are discussed in the context of neutron diffraction thermal parameters and an STO-3G calculation of the field gradients at the two sites. Although the temperature dependence is qualitatively in agreement with the structure data, the discrepancy between the calculated and observed asymmetry parameters, particularly for site I, suggests that hydrogen bonding to sulfate is an important feature in determining the ammonium ion charge distribution and hence the field gradient tensor at nitrogen. At 296.1 K the coupling parameters are e*qQ/h (I) = 154.53 kHz, n(I) =0.684; e2qQ/h (II) = 115.71 kHz, ~(11) =0.749.
Proceedings of the National Academy of Sciences of the United States of America, 1982
We have used 2H quadrupole-echo NMR spectroscopy to study the molecular dynamics of the leucine s... more We have used 2H quadrupole-echo NMR spectroscopy to study the molecular dynamics of the leucine side chain in collagen fibrils labeled with [2H10]leucine. X-ray crystallographic studies ofleucine and small leucyl-containing peptides and proteins [Benedetti, C. (1977) in Proceedings ofthe Fifth American Peptides Symposium, eds.
Journal of the American Chemical Society, Apr 1, 1983
Chemischer Informationsdienst, Aug 2, 1983
Encyclopedia of Magnetic Resonance, Mar 15, 2007
The study of 2 H NMR in the solid state offers one method to probe molecular structure and dynami... more The study of 2 H NMR in the solid state offers one method to probe molecular structure and dynamics in solids. This article will describe the details of the method with particular emphasis on the nature of the quadrupolar coupling of the 2 H nucleus with a surrounding ...
Biophysical Journal, Oct 1, 1980
Collagen was labeled with [3,3,3-d3]alanine and with [d10]leucine via tissue culture. 2H nuclear ... more Collagen was labeled with [3,3,3-d3]alanine and with [d10]leucine via tissue culture. 2H nuclear magnetic resonance (NMR) spectra were obtained of collagelt in solution and as fibrils using the quadrupolar echo technique. The 2H NMR data for [3,3,3-d3]alanine-labeled collagen fibrils were analyzed in terms of a model for motion in which the molecule is considered to jump between two sites, separated azimuthally by an angle 26, in a time which is rapid compared with the residence time in both sites. The data suggest that the molecule undergoes reorientation over an angle, 2b, of-300 in the fibrils, and that the average angle between the alanine C"-C, bond axis and the long axis of the helix is-750. Reorientation is possibly segmental. The T2 for [3,3,3-d3]alanine-labeled collagen ribrils was estimated to be 105 ,us. The 2H NMR data for the methyl groups of [d10]leucine-labeled collagen were analyzed qualitatively. These data established that for collagen in solution and as fibrils, rotation occurs about the leucine side-chain bonds, in addition to threefold methyl rotation and reorientation of the peptide backbone. The T2 for the methyl groups of leucine-labeled collagen is estimated to be-130 ,is. Taken together, these data provide strong evidence that both polypeptide backbone reorientation and amino acid side-chain motion occur in collagen molecules in the fibrils. Stabilizing interactions that determine fibril structure must therefore depend upon at least two sets of contacts in any given local region.
Chemischer Informationsdienst, Aug 18, 1981
Novartis Foundation Symposium, May 30, 2008
13C- and 2H-labelled amino acids have been incorporated into elastin and collagen and rotational ... more 13C- and 2H-labelled amino acids have been incorporated into elastin and collagen and rotational correlation times of the labelled sites have been derived from an analysis of nuclear magnetic resonance relaxation parameters and line-shapes. The elastin experiments were designed to discriminate between the various models that have been proposed to account for the rubber-like elasticity of elastin. The correlation times of carbonyl carbons of the elastin backbone show that elastin chains are very flexible at the molecular level. In addition, the molecular dynamics and viscoelastic behaviour of elastin are well correlated over a wide range of temperatures and solvents. These results all support the rubber-like network model of elastin structure. The collagen experiments were designed to investigate the intermolecular interactions between molecules in collagen fibres. Correlation times of labelled sites in the collagen backbone and side-chains show that substantial flexibility, especially of the side-chains, takes place in reconstituted (non-cross-linked) collagen fibrils. Therefore, the interactions between side-chains that presumably direct and stabilize the fibrillar assembly take place in fluid domains. The molecular flexibility is not affected by the presence of cross-links but is absent when the collagen is mineralized.
Encyclopedia of Magnetic Resonance, 2007
The study of 2 H NMR in the solid state offers one method to probe molecular structure and dynami... more The study of 2 H NMR in the solid state offers one method to probe molecular structure and dynamics in solids. This article will describe the details of the method with particular emphasis on the nature of the quadrupolar coupling of the 2 H nucleus with a surrounding ...
Proceedings of the National Academy of Sciences, 1982
We have used 2H quadrupole-echo NMR spectroscopy to study the molecular dynamics of the leucine s... more We have used 2H quadrupole-echo NMR spectroscopy to study the molecular dynamics of the leucine side chain in collagen fibrils labeled with [2H10]leucine. X-ray crystallographic studies of leucine and small leucyl-containing peptides and proteins [Benedetti, C. (1977) in Proceedings of the Fifth American Peptides Symposium, eds, Goodman, M. & Meienhofer, J. (Wiley, New York), pp. 257--274; Janin, J., Wodak, S., Levitt, M. & Maigret, B. (1978) J. Mol. Biol. 125, 357--386] show that the amino acid side chain exists predominantly in only two of the nine possible conformations. 2H NMR spectra of polycrystalline D,L [2H10]leucine obtained from -45 degrees C to +100 degrees C showed that interconversion of the two conformations did not take place on the 2H NMR timescale in this temperature range. In contrast, experimental lineshapes observed for [2H10]leucine-labeled collagen fibrils from -85 degrees C to +30 degrees C were simulated by using a model in which the side chain hops at variou...
Journal of the American Chemical Society, 2008
Journal of the American Chemical Society, 1983
The Journal of Chemical Physics, 1981
The pure nuclear quadrupole spectrum of deuterium at oxygen in chlorinated phenols has been obser... more The pure nuclear quadrupole spectrum of deuterium at oxygen in chlorinated phenols has been observed by level crossing double resonance with the ring protons. Observed coupling constants, ranging from 200 to 250 kHz, exhibit the effects of strong hydrogen bonding through their correlation with the intermolecular O–H⋅⋅⋅O bond lengths in those cases where structure data are available. This is interpreted below to indicate that a primary effect of chlorine substitution is the influence it exerts on intermolecular hydrogen bonding through modification of the barrier to hydroxyl group rotation. From an extrapolation of the observed distance dependence, one may obtain a coupling constant of ∼283 kHz for deuterium at the oxygen position in non-hydrogen-bonded phenol. An interpretation of these data is made using model calculations on phenol, vinyl alcohol, and chlorovinyl alcohol. Barriers to internal rotation, as well as the dependence of the deuterium quadrupole coupling constant on the ...
Journal of magnetic resonance, Feb 1, 1980
The quadrupole coupling parameters for i4N in the two chemically inequivalent sites in paraelectr... more The quadrupole coupling parameters for i4N in the two chemically inequivalent sites in paraelectric ammonium sulfate have been measured by proton-nitrogen double resonance for the interval 225 K 5 TZ 365 K. Transition frequencies are represented to within ca. 0.2 kHz in this interval by Y+ (1)=242.43-0.33807; V-(I) = 144.03-0.1855 T; V+ (II) = 147.08-0.1294 T; V-(II) = 73.39-0.0281 T kHz, where T is the temperature in degrees Kelvin. These data are discussed in the context of neutron diffraction thermal parameters and an STO-3G calculation of the field gradients at the two sites. Although the temperature dependence is qualitatively in agreement with the structure data, the discrepancy between the calculated and observed asymmetry parameters, particularly for site I, suggests that hydrogen bonding to sulfate is an important feature in determining the ammonium ion charge distribution and hence the field gradient tensor at nitrogen. At 296.1 K the coupling parameters are e*qQ/h (I) = 154.53 kHz, n(I) =0.684; e2qQ/h (II) = 115.71 kHz, ~(11) =0.749.
Proceedings of the National Academy of Sciences of the United States of America, 1982
We have used 2H quadrupole-echo NMR spectroscopy to study the molecular dynamics of the leucine s... more We have used 2H quadrupole-echo NMR spectroscopy to study the molecular dynamics of the leucine side chain in collagen fibrils labeled with [2H10]leucine. X-ray crystallographic studies ofleucine and small leucyl-containing peptides and proteins [Benedetti, C. (1977) in Proceedings ofthe Fifth American Peptides Symposium, eds.
Journal of the American Chemical Society, Apr 1, 1983
Chemischer Informationsdienst, Aug 2, 1983
Encyclopedia of Magnetic Resonance, Mar 15, 2007
The study of 2 H NMR in the solid state offers one method to probe molecular structure and dynami... more The study of 2 H NMR in the solid state offers one method to probe molecular structure and dynamics in solids. This article will describe the details of the method with particular emphasis on the nature of the quadrupolar coupling of the 2 H nucleus with a surrounding ...
Biophysical Journal, Oct 1, 1980
Collagen was labeled with [3,3,3-d3]alanine and with [d10]leucine via tissue culture. 2H nuclear ... more Collagen was labeled with [3,3,3-d3]alanine and with [d10]leucine via tissue culture. 2H nuclear magnetic resonance (NMR) spectra were obtained of collagelt in solution and as fibrils using the quadrupolar echo technique. The 2H NMR data for [3,3,3-d3]alanine-labeled collagen fibrils were analyzed in terms of a model for motion in which the molecule is considered to jump between two sites, separated azimuthally by an angle 26, in a time which is rapid compared with the residence time in both sites. The data suggest that the molecule undergoes reorientation over an angle, 2b, of-300 in the fibrils, and that the average angle between the alanine C"-C, bond axis and the long axis of the helix is-750. Reorientation is possibly segmental. The T2 for [3,3,3-d3]alanine-labeled collagen ribrils was estimated to be 105 ,us. The 2H NMR data for the methyl groups of [d10]leucine-labeled collagen were analyzed qualitatively. These data established that for collagen in solution and as fibrils, rotation occurs about the leucine side-chain bonds, in addition to threefold methyl rotation and reorientation of the peptide backbone. The T2 for the methyl groups of leucine-labeled collagen is estimated to be-130 ,is. Taken together, these data provide strong evidence that both polypeptide backbone reorientation and amino acid side-chain motion occur in collagen molecules in the fibrils. Stabilizing interactions that determine fibril structure must therefore depend upon at least two sets of contacts in any given local region.
Chemischer Informationsdienst, Aug 18, 1981
Novartis Foundation Symposium, May 30, 2008
13C- and 2H-labelled amino acids have been incorporated into elastin and collagen and rotational ... more 13C- and 2H-labelled amino acids have been incorporated into elastin and collagen and rotational correlation times of the labelled sites have been derived from an analysis of nuclear magnetic resonance relaxation parameters and line-shapes. The elastin experiments were designed to discriminate between the various models that have been proposed to account for the rubber-like elasticity of elastin. The correlation times of carbonyl carbons of the elastin backbone show that elastin chains are very flexible at the molecular level. In addition, the molecular dynamics and viscoelastic behaviour of elastin are well correlated over a wide range of temperatures and solvents. These results all support the rubber-like network model of elastin structure. The collagen experiments were designed to investigate the intermolecular interactions between molecules in collagen fibres. Correlation times of labelled sites in the collagen backbone and side-chains show that substantial flexibility, especially of the side-chains, takes place in reconstituted (non-cross-linked) collagen fibrils. Therefore, the interactions between side-chains that presumably direct and stabilize the fibrillar assembly take place in fluid domains. The molecular flexibility is not affected by the presence of cross-links but is absent when the collagen is mineralized.
Encyclopedia of Magnetic Resonance, 2007
The study of 2 H NMR in the solid state offers one method to probe molecular structure and dynami... more The study of 2 H NMR in the solid state offers one method to probe molecular structure and dynamics in solids. This article will describe the details of the method with particular emphasis on the nature of the quadrupolar coupling of the 2 H nucleus with a surrounding ...
Proceedings of the National Academy of Sciences, 1982
We have used 2H quadrupole-echo NMR spectroscopy to study the molecular dynamics of the leucine s... more We have used 2H quadrupole-echo NMR spectroscopy to study the molecular dynamics of the leucine side chain in collagen fibrils labeled with [2H10]leucine. X-ray crystallographic studies of leucine and small leucyl-containing peptides and proteins [Benedetti, C. (1977) in Proceedings of the Fifth American Peptides Symposium, eds, Goodman, M. & Meienhofer, J. (Wiley, New York), pp. 257--274; Janin, J., Wodak, S., Levitt, M. & Maigret, B. (1978) J. Mol. Biol. 125, 357--386] show that the amino acid side chain exists predominantly in only two of the nine possible conformations. 2H NMR spectra of polycrystalline D,L [2H10]leucine obtained from -45 degrees C to +100 degrees C showed that interconversion of the two conformations did not take place on the 2H NMR timescale in this temperature range. In contrast, experimental lineshapes observed for [2H10]leucine-labeled collagen fibrils from -85 degrees C to +30 degrees C were simulated by using a model in which the side chain hops at variou...
Journal of the American Chemical Society, 2008
Journal of the American Chemical Society, 1983
The Journal of Chemical Physics, 1981
The pure nuclear quadrupole spectrum of deuterium at oxygen in chlorinated phenols has been obser... more The pure nuclear quadrupole spectrum of deuterium at oxygen in chlorinated phenols has been observed by level crossing double resonance with the ring protons. Observed coupling constants, ranging from 200 to 250 kHz, exhibit the effects of strong hydrogen bonding through their correlation with the intermolecular O–H⋅⋅⋅O bond lengths in those cases where structure data are available. This is interpreted below to indicate that a primary effect of chlorine substitution is the influence it exerts on intermolecular hydrogen bonding through modification of the barrier to hydroxyl group rotation. From an extrapolation of the observed distance dependence, one may obtain a coupling constant of ∼283 kHz for deuterium at the oxygen position in non-hydrogen-bonded phenol. An interpretation of these data is made using model calculations on phenol, vinyl alcohol, and chlorovinyl alcohol. Barriers to internal rotation, as well as the dependence of the deuterium quadrupole coupling constant on the ...