Abstract
A major limitation of solution NMR is molecular tumbling, which is often too slow for detection. Here we demonstrate that solid-state NMR spectroscopy in combination with flash freezing of cells can be used to detect proteins in the cellular environment and provides information on backbone chemical shifts.
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Escherichia coli / chemistry
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Escherichia coli / cytology
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Humans
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Molecular Weight
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Nuclear Magnetic Resonance, Biomolecular*
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Tacrolimus Binding Protein 1A / chemistry*
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Tacrolimus Binding Protein 1A / metabolism
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Thioredoxins / chemistry*
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Thioredoxins / metabolism
Substances
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Thioredoxins
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Tacrolimus Binding Protein 1A