1H-filtered correlation experiments for assignment and determination of coupling constants in backbone labelled proteins

1H-filtered correlation experiments for assignment and determination of coupling constants in backbone labelled proteins

The implementation of [13Calpha,13C',15N,2Halpha] labelled amino acids into proteins allows the acquisition of high resolution triple resonance experiments. We present for the first time resonance assignments facilitated by this new labelling strategy. The absence of 1JCalpha,Cbeta couplings en...

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Veröffentlicht in:Journal of biomolecular NMR 2002-01, Vol.22 (1), p.21-26
Hauptverfasser: Giesen, Alexander W, Bae, Lynnette C, Barrett, Christa L, Chyba, Jason A, Chaykovsky, Michael M, Cheng, Minn-Chang, Murray, Jenny H, Oliver, Ed J, Sullivan, Sarah M, Brown, Jonathan Miles, Homans, Steve W
Format: Artikel
Sprache:eng
Schlagworte:
Amides
Amino acids
Anisotropy
Carbon Isotopes
Deuterium
Experiments
Half-Life
Magnetics
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular - methods
Proteins - chemistry
Protons
Resonance
Sensitivity and Specificity
Ubiquitin - chemistry
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Zusammenfassung:The implementation of [13Calpha,13C',15N,2Halpha] labelled amino acids into proteins allows the acquisition of high resolution triple resonance experiments. We present for the first time resonance assignments facilitated by this new labelling strategy. The absence of 1JCalpha,Cbeta couplings enables us to measure 1JCalpha,C' scalar and 1DCalpha,C' residual dipolar coupling constants using modified HNCA experiments which do not suffer from sensitivity losses characteristic for 13C constant time experiments.
ISSN:0925-2738
1573-5001
DOI:10.1023/A:1013831417615