{"_id":"8491","type":"journal_article","page":"199-211","article_type":"original","doi":"10.1007/s10858-005-4425-x","publication_status":"published","issue":"4","publication":"Journal of Biomolecular NMR","language":[{"iso":"eng"}],"status":"public","date_created":"2020-09-18T10:13:59Z","author":[{"first_name":"Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"last_name":"Kupče","first_name":"Ēriks","full_name":"Kupče, Ēriks"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"}],"oa_version":"None","abstract":[{"lang":"eng","text":"Fast multidimensional NMR with a time resolution of a few seconds provides a new tool for high throughput screening and site-resolved real-time studies of kinetic molecular processes by NMR. Recently we have demonstrated the feasibility to record protein 1H–15N correlation spectra in a few seconds of acquisition time using a new SOFAST-HMQC experiment (Schanda and Brutscher (2005) J. Am. Chem. Soc. 127, 8014). Here, we investigate in detail the performance of SOFAST-HMQC to record 1H–15N and 1H−13C correlation spectra of proteins of different size and at different magnetic field strengths. Compared to standard 1H–15N correlation experiments SOFAST-HMQC provides a significant gain in sensitivity, especially for fast repetition rates. Guidelines are provided on how to set up SOFAST-HMQC experiments for a given protein sample. In addition, an alternative pulse scheme, IPAP-SOFAST-HMQC is presented that allows application on NMR spectrometers equipped with cryogenic probes, and fast measurement of one-bond 1H–13C and 1H–15N scalar and residual dipolar coupling constants."}],"volume":33,"date_updated":"2021-01-12T08:19:38Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","month":"12","article_processing_charge":"No","year":"2005","publication_identifier":{"issn":["0925-2738","1573-5001"]},"publisher":"Springer Nature","day":"01","quality_controlled":"1","keyword":["Spectroscopy","Biochemistry"],"title":"SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds","intvolume":"        33","date_published":"2005-12-01T00:00:00Z","extern":"1","citation":{"chicago":"Schanda, Paul, Ēriks Kupče, and Bernhard Brutscher. “SOFAST-HMQC Experiments for Recording Two-Dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds.” <i>Journal of Biomolecular NMR</i>. Springer Nature, 2005. <a href=\"https://doi.org/10.1007/s10858-005-4425-x\">https://doi.org/10.1007/s10858-005-4425-x</a>.","ista":"Schanda P, Kupče Ē, Brutscher B. 2005. SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. Journal of Biomolecular NMR. 33(4), 199–211.","apa":"Schanda, P., Kupče, Ē., &#38; Brutscher, B. (2005). SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. <i>Journal of Biomolecular NMR</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s10858-005-4425-x\">https://doi.org/10.1007/s10858-005-4425-x</a>","short":"P. Schanda, Ē. Kupče, B. Brutscher, Journal of Biomolecular NMR 33 (2005) 199–211.","mla":"Schanda, Paul, et al. “SOFAST-HMQC Experiments for Recording Two-Dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds.” <i>Journal of Biomolecular NMR</i>, vol. 33, no. 4, Springer Nature, 2005, pp. 199–211, doi:<a href=\"https://doi.org/10.1007/s10858-005-4425-x\">10.1007/s10858-005-4425-x</a>.","ama":"Schanda P, Kupče Ē, Brutscher B. SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. <i>Journal of Biomolecular NMR</i>. 2005;33(4):199-211. doi:<a href=\"https://doi.org/10.1007/s10858-005-4425-x\">10.1007/s10858-005-4425-x</a>","ieee":"P. Schanda, Ē. Kupče, and B. Brutscher, “SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds,” <i>Journal of Biomolecular NMR</i>, vol. 33, no. 4. Springer Nature, pp. 199–211, 2005."}}