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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 |
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| Personen und Körperschaften: | , |
| In: | Concepts in Magnetic Resonance Part A, 42A, 2013, 1, S. 14-22 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| Zusammenfassung: | <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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| Umfang: | 14-22 |
| ISSN: |
1546-6086
1552-5023 |
| DOI: | 10.1002/cmr.a.21254 |