Abstract
In this communication a new NMR experiment for the safe observation and quantification of water-protein exchange phenomena is presented. It combines a water-selective pulse, offering chemical shift-based separation, and the off-resonance ROESY dynamic filter, which permits the elimination of the unwanted intramolecular dipolar cross relaxation of protein protons. Moreover, pulsed field gradients are used for the suppression of radiation damping and the solvent signal. The straightforward incorporation of this sequence in heteronuclear experiments is demonstrated for the case of the DNA-binding domain of the alcohol regulator protein.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Aprotinin / chemistry
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Aspergillus nidulans / chemistry
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Aspergillus nidulans / metabolism
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Binding Sites
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Cattle
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DNA, Fungal / metabolism*
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / metabolism*
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Evaluation Studies as Topic
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Fungal Proteins / chemistry*
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Fungal Proteins / metabolism*
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Magnetic Resonance Spectroscopy / methods*
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Molecular Structure
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Transcription Factors / chemistry*
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Transcription Factors / metabolism*
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Water
Substances
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ALCR protein, Aspergillus nidulans
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DNA, Fungal
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DNA-Binding Proteins
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Fungal Proteins
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Transcription Factors
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Water
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Aprotinin