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1H-filtered correlation experiments for assignment and determination of coupling constants in backbone labelled proteins.
- Source :
- Journal of Biomolecular NMR; Jan2002, Vol. 22 Issue 1, p21-26, 6p
- Publication Year :
- 2002
-
Abstract
- The implementation of [<superscript>13</superscript>Cα,<superscript>13</superscript>C′,<superscript>15</superscript>N,<superscript>2</superscript>Hα] 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 <superscript>1</superscript>J<subscript>Cα,Cβ</subscript> couplings enables us to measure <superscript>1</superscript>J<subscript>Cα,C′</subscript> scalar and <superscript>1</superscript>D<subscript>Cα,C′</subscript> residual dipolar coupling constants using modified HNCA experiments which do not suffer from sensitivity losses characteristic for <superscript>13</superscript>C constant time experiments. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09252738
- Volume :
- 22
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Journal of Biomolecular NMR
- Publication Type :
- Academic Journal
- Accession number :
- 15608768
- Full Text :
- https://doi.org/10.1023/A:1013831417615