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<titleInfo><title>Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons</title></titleInfo>


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<name type="personal">
  <namePart type="given">Paul</namePart>
  <namePart type="family">Schanda</namePart>
  <role><roleTerm type="text">author</roleTerm> </role><identifier type="local">7B541462-FAF6-11E9-A490-E8DFE5697425</identifier><description xsi:type="identifierDefinition" type="orcid">0000-0002-9350-7606</description></name>
<name type="personal">
  <namePart type="given">Ewen</namePart>
  <namePart type="family">Lescop</namePart>
  <role><roleTerm type="text">author</roleTerm> </role></name>
<name type="personal">
  <namePart type="given">Mirjam</namePart>
  <namePart type="family">Falge</namePart>
  <role><roleTerm type="text">author</roleTerm> </role></name>
<name type="personal">
  <namePart type="given">Rémy</namePart>
  <namePart type="family">Sounier</namePart>
  <role><roleTerm type="text">author</roleTerm> </role></name>
<name type="personal">
  <namePart type="given">Jérôme</namePart>
  <namePart type="family">Boisbouvier</namePart>
  <role><roleTerm type="text">author</roleTerm> </role></name>
<name type="personal">
  <namePart type="given">Bernhard</namePart>
  <namePart type="family">Brutscher</namePart>
  <role><roleTerm type="text">author</roleTerm> </role></name>














<abstract lang="eng">High signal to noise is a necessity for the quantification of NMR spectral parameters to be translated into accurate and precise restraints on protein structure and dynamics. An important source of long-range structural information is obtained from 1H–1H residual dipolar couplings (RDCs) measured for weakly aligned molecules. For sensitivity reasons, such measurements are generally performed on highly deuterated protein samples. Here we show that high sensitivity is also obtained for protonated protein samples if the pulse schemes are optimized in terms of longitudinal relaxation efficiency and J-mismatch compensated coherence transfer. The new sensitivity-optimized quantitative J-correlation experiment yields important signal gains reaching factors of 1.5 to 8 for individual correlation peaks when compared to previously proposed pulse schemes.</abstract>

<originInfo><publisher>Springer Nature</publisher><dateIssued encoding="w3cdtf">2007</dateIssued>
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<language><languageTerm authority="iso639-2b" type="code">eng</languageTerm>
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<subject><topic>Spectroscopy</topic><topic>Biochemistry</topic>
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<relatedItem type="host"><titleInfo><title>Journal of Biomolecular NMR</title></titleInfo>
  <identifier type="issn">0925-2738</identifier>
  <identifier type="issn">1573-5001</identifier><identifier type="doi">10.1007/s10858-006-9138-2</identifier>
<part><detail type="volume"><number>38</number></detail><extent unit="pages">47-55</extent>
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<apa>Schanda, P., Lescop, E., Falge, M., Sounier, R., Boisbouvier, J., &amp;#38; Brutscher, B. (2007). Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. &lt;i&gt;Journal of Biomolecular NMR&lt;/i&gt;. Springer Nature. &lt;a href=&quot;https://doi.org/10.1007/s10858-006-9138-2&quot;&gt;https://doi.org/10.1007/s10858-006-9138-2&lt;/a&gt;</apa>
<mla>Schanda, Paul, et al. “Sensitivity-Optimized Experiment for the Measurement of Residual Dipolar Couplings between Amide Protons.” &lt;i&gt;Journal of Biomolecular NMR&lt;/i&gt;, vol. 38, Springer Nature, 2007, pp. 47–55, doi:&lt;a href=&quot;https://doi.org/10.1007/s10858-006-9138-2&quot;&gt;10.1007/s10858-006-9138-2&lt;/a&gt;.</mla>
<ieee>P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, and B. Brutscher, “Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons,” &lt;i&gt;Journal of Biomolecular NMR&lt;/i&gt;, vol. 38. Springer Nature, pp. 47–55, 2007.</ieee>
<chicago>Schanda, Paul, Ewen Lescop, Mirjam Falge, Rémy Sounier, Jérôme Boisbouvier, and Bernhard Brutscher. “Sensitivity-Optimized Experiment for the Measurement of Residual Dipolar Couplings between Amide Protons.” &lt;i&gt;Journal of Biomolecular NMR&lt;/i&gt;. Springer Nature, 2007. &lt;a href=&quot;https://doi.org/10.1007/s10858-006-9138-2&quot;&gt;https://doi.org/10.1007/s10858-006-9138-2&lt;/a&gt;.</chicago>
<short>P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, B. Brutscher, Journal of Biomolecular NMR 38 (2007) 47–55.</short>
<ista>Schanda P, Lescop E, Falge M, Sounier R, Boisbouvier J, Brutscher B. 2007. Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. Journal of Biomolecular NMR. 38, 47–55.</ista>
<ama>Schanda P, Lescop E, Falge M, Sounier R, Boisbouvier J, Brutscher B. Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. &lt;i&gt;Journal of Biomolecular NMR&lt;/i&gt;. 2007;38:47-55. doi:&lt;a href=&quot;https://doi.org/10.1007/s10858-006-9138-2&quot;&gt;10.1007/s10858-006-9138-2&lt;/a&gt;</ama>
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