Improved HSQC experiments for the observation of exchange broadened signals

F A Mulder; C A Spronk; M Slijper; R Kaptein; R Boelens

doi:10.1007/BF00211169

Improved HSQC experiments for the observation of exchange broadened signals

F A Mulder, C A Spronk, M Slijper, R Kaptein, R Boelens

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

We present here HSQC experiments with improved sensitivity for signals in the presence of exchange broadening. During periods of coherence transfer through scalar coupling the experiments employ CPMG-derived pulse trains to reduce loss of dephasing of spin coherence due to chemical exchange. (15)N-(1)H gradient CPMG-HSQC and SE-CPMG-HSQC experiments have been developed and applied to complexes of lac repressor headpiece with operator DNA. Improved sensitivity is demonstrated for many protein backbone and side-chain resonances in the complex, markedly for signals of protons located at the protein-DNA interface. In addition, a significant increase in intensity is observed for arginine guanidino groups undergoing conformational exchange.

Original language	English
Pages (from-to)	223-8
Number of pages	6
Journal	Journal of Biomolecular NMR
Volume	8
Issue number	2
DOIs	https://doi.org/10.1007/BF00211169
Publication status	Published - Sept 1996

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10.1007/BF00211169

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abstract = "We present here HSQC experiments with improved sensitivity for signals in the presence of exchange broadening. During periods of coherence transfer through scalar coupling the experiments employ CPMG-derived pulse trains to reduce loss of dephasing of spin coherence due to chemical exchange. (15)N-(1)H gradient CPMG-HSQC and SE-CPMG-HSQC experiments have been developed and applied to complexes of lac repressor headpiece with operator DNA. Improved sensitivity is demonstrated for many protein backbone and side-chain resonances in the complex, markedly for signals of protons located at the protein-DNA interface. In addition, a significant increase in intensity is observed for arginine guanidino groups undergoing conformational exchange.",

author = "Mulder, {F A} and Spronk, {C A} and M Slijper and R Kaptein and R Boelens",

year = "1996",

month = sep,

doi = "10.1007/BF00211169",

language = "English",

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T1 - Improved HSQC experiments for the observation of exchange broadened signals

AU - Mulder, F A

AU - Spronk, C A

AU - Slijper, M

AU - Kaptein, R

AU - Boelens, R

PY - 1996/9

Y1 - 1996/9

N2 - We present here HSQC experiments with improved sensitivity for signals in the presence of exchange broadening. During periods of coherence transfer through scalar coupling the experiments employ CPMG-derived pulse trains to reduce loss of dephasing of spin coherence due to chemical exchange. (15)N-(1)H gradient CPMG-HSQC and SE-CPMG-HSQC experiments have been developed and applied to complexes of lac repressor headpiece with operator DNA. Improved sensitivity is demonstrated for many protein backbone and side-chain resonances in the complex, markedly for signals of protons located at the protein-DNA interface. In addition, a significant increase in intensity is observed for arginine guanidino groups undergoing conformational exchange.

AB - We present here HSQC experiments with improved sensitivity for signals in the presence of exchange broadening. During periods of coherence transfer through scalar coupling the experiments employ CPMG-derived pulse trains to reduce loss of dephasing of spin coherence due to chemical exchange. (15)N-(1)H gradient CPMG-HSQC and SE-CPMG-HSQC experiments have been developed and applied to complexes of lac repressor headpiece with operator DNA. Improved sensitivity is demonstrated for many protein backbone and side-chain resonances in the complex, markedly for signals of protons located at the protein-DNA interface. In addition, a significant increase in intensity is observed for arginine guanidino groups undergoing conformational exchange.

U2 - 10.1007/BF00211169

DO - 10.1007/BF00211169

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SP - 223

EP - 228

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

IS - 2

ER -

Improved HSQC experiments for the observation of exchange broadened signals

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