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Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride
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| Zeitschriftentitel: | Concepts in Magnetic Resonance Part A |
|---|---|
| Personen und Körperschaften: | , |
| In: | Concepts in Magnetic Resonance Part A, 42A, 2013, 1, S. 14-22 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
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Li, Wenbo Mcdermott, Ann E. Li, Wenbo Mcdermott, Ann E. |
|---|---|
| author |
Li, Wenbo Mcdermott, Ann E. |
| spellingShingle |
Li, Wenbo Mcdermott, Ann E. Concepts in Magnetic Resonance Part A Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride Spectroscopy |
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li, wenbo |
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Li, Wenbo Mcdermott, Ann E. 1546-6086 1552-5023 Wiley Spectroscopy http://dx.doi.org/10.1002/cmr.a.21254 <jats:title>Abstract</jats:title><jats:p>New methods for probing dynamical properties of biological macromolecules on the millisecond timescale will enable a better understanding of the structure–function relationship. In this article, three solid‐state NMR detection methods, line‐shape analysis, two‐dimensional exchange experiments, and a variant of the center‐band only detection of exchange (CODEX) experiment called R‐CODEX, are used to characterize a crystalline amino acid that serves as a model for motions in solid proteins, <jats:sc>L</jats:sc>‐phenylalanine hydrochloride. The millisecond ring flip motion of the aromatic ring in <jats:sc>L</jats:sc>‐phenylalanine hydrochloride is characterized in detail for the first time. Limitations of these experiments for processes involving submillisecond timescales are also discussed. © 2013 Wiley Periodicals, Inc. Concepts Magn Reson Part A 42A: 14–22, 2013.</jats:p> Detection of slow dynamics by solid‐state NMR: Application to <scp>L</scp>‐phenylalanine hydrochloride Concepts in Magnetic Resonance Part A |
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| title |
Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_unstemmed |
Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_full |
Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_fullStr |
Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_full_unstemmed |
Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_short |
Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_sort |
detection of slow dynamics by solid‐state nmr: application to <scp>l</scp>‐phenylalanine hydrochloride |
| topic |
Spectroscopy |
| url |
http://dx.doi.org/10.1002/cmr.a.21254 |
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2013 |
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14-22 |
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<jats:title>Abstract</jats:title><jats:p>New methods for probing dynamical properties of biological macromolecules on the millisecond timescale will enable a better understanding of the structure–function relationship. In this article, three solid‐state NMR detection methods, line‐shape analysis, two‐dimensional exchange experiments, and a variant of the center‐band only detection of exchange (CODEX) experiment called R‐CODEX, are used to characterize a crystalline amino acid that serves as a model for motions in solid proteins, <jats:sc>L</jats:sc>‐phenylalanine hydrochloride. The millisecond ring flip motion of the aromatic ring in <jats:sc>L</jats:sc>‐phenylalanine hydrochloride is characterized in detail for the first time. Limitations of these experiments for processes involving submillisecond timescales are also discussed. © 2013 Wiley Periodicals, Inc. Concepts Magn Reson Part A 42A: 14–22, 2013.</jats:p> |
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| description | <jats:title>Abstract</jats:title><jats:p>New methods for probing dynamical properties of biological macromolecules on the millisecond timescale will enable a better understanding of the structure–function relationship. In this article, three solid‐state NMR detection methods, line‐shape analysis, two‐dimensional exchange experiments, and a variant of the center‐band only detection of exchange (CODEX) experiment called R‐CODEX, are used to characterize a crystalline amino acid that serves as a model for motions in solid proteins, <jats:sc>L</jats:sc>‐phenylalanine hydrochloride. The millisecond ring flip motion of the aromatic ring in <jats:sc>L</jats:sc>‐phenylalanine hydrochloride is characterized in detail for the first time. Limitations of these experiments for processes involving submillisecond timescales are also discussed. © 2013 Wiley Periodicals, Inc. Concepts Magn Reson Part A 42A: 14–22, 2013.</jats:p> |
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| spelling | Li, Wenbo Mcdermott, Ann E. 1546-6086 1552-5023 Wiley Spectroscopy http://dx.doi.org/10.1002/cmr.a.21254 <jats:title>Abstract</jats:title><jats:p>New methods for probing dynamical properties of biological macromolecules on the millisecond timescale will enable a better understanding of the structure–function relationship. In this article, three solid‐state NMR detection methods, line‐shape analysis, two‐dimensional exchange experiments, and a variant of the center‐band only detection of exchange (CODEX) experiment called R‐CODEX, are used to characterize a crystalline amino acid that serves as a model for motions in solid proteins, <jats:sc>L</jats:sc>‐phenylalanine hydrochloride. The millisecond ring flip motion of the aromatic ring in <jats:sc>L</jats:sc>‐phenylalanine hydrochloride is characterized in detail for the first time. Limitations of these experiments for processes involving submillisecond timescales are also discussed. © 2013 Wiley Periodicals, Inc. Concepts Magn Reson Part A 42A: 14–22, 2013.</jats:p> Detection of slow dynamics by solid‐state NMR: Application to <scp>L</scp>‐phenylalanine hydrochloride Concepts in Magnetic Resonance Part A |
| spellingShingle | Li, Wenbo, Mcdermott, Ann E., Concepts in Magnetic Resonance Part A, Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride, Spectroscopy |
| title | Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_full | Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_fullStr | Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_full_unstemmed | Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_short | Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| title_sort | detection of slow dynamics by solid‐state nmr: application to <scp>l</scp>‐phenylalanine hydrochloride |
| title_unstemmed | Detection of slow dynamics by solid‐state NMR: Application to L‐phenylalanine hydrochloride |
| topic | Spectroscopy |
| url | http://dx.doi.org/10.1002/cmr.a.21254 |