We are analyzing https://link.springer.com/article/10.1007/s10858-005-4425-x.

Title:
SOFAST-HMQC Experiments for Recording Two-dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds | Journal of Biomolecular NMR
Description:
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.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Mobile Technology & AI
Telecommunications

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 7,642,828 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We don't see any clear sign of profit-making.

Not all websites are made for profit; some exist to inform or educate users. Or any other reason why people make websites. And this might be the case. Link.springer.com might be cashing in, but we can't detect the method they're using.

Keywords {🔍}

google, scholar, article, cas, nmr, reson, chem, soc, magn, brutscher, kupče, sofasthmqc, correlation, privacy, cookies, content, journal, experiments, schanda, magnetic, access, biomol, freeman, publish, search, spectra, proteins, seconds, protein, data, information, log, research, twodimensional, bernhard, discover, resonance, szyperski, usa, nucl, download, author, springer, optional, analysis, personal, parties, policy, find, track,

Topics {✒️}

site-resolved real-time studies 1h−13c correlation spectra month download article/chapter nuclear magnetic resonance umr5075 cnrs-cea-ujf sofast-hmqc experiments related subjects record 1h–15n sofast-hmqc experiment ipap-sofast-hmqc fast repetition rates bond 1h–13c biomolecular nmr aims full article pdf 1h–15n scalar privacy choices/manage cookies magnetic field strengths protein sample nmr spectrometers equipped seconds article published check access instant access sofast-hmqc sofast-hmqc european economic area high throughput screening kinetic molecular processes alternative pulse scheme rue jules horowitz conditions privacy policy article schanda article journal accepting optional cookies bernhard brutscher fast measurement journal finder publish main content log ernst author correspondence article log article cite magnetic res selectively [1h privacy policy biomol nmr 33 personal data books a optional cookies usage analysis manage preferences

Schema {🗺️}

WebPage:
      mainEntity:
         headline:SOFAST-HMQC Experiments for Recording Two-dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds
         description: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.
         datePublished:
         dateModified:
         pageStart:199
         pageEnd:211
         sameAs:https://doi.org/10.1007/s10858-005-4425-x
         keywords:
            Ernst angle
            fast NMR
            HMQC
            longitudinal relaxation enhancement
            protein
            residual dipolar couplings
            Biological and Medical Physics
            Biophysics
            Biochemistry
            general
            Spectroscopy/Spectrometry
         image:
         isPartOf:
            name:Journal of Biomolecular NMR
            issn:
               1573-5001
               0925-2738
            volumeNumber:33
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Kluwer Academic Publishers
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Paul Schanda
               affiliation:
                     name:UMR5075 CNRS-CEA-UJF
                     address:
                        name:Institut de Biologie Structurale – Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, Grenoble Cedex, France
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Ēriks Kupče
               affiliation:
                     name:Walton-on-Thames
                     address:
                        name:Varian Ltd., Walton-on-Thames, Surrey, United Kingdom
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Bernhard Brutscher
               affiliation:
                     name:UMR5075 CNRS-CEA-UJF
                     address:
                        name:Institut de Biologie Structurale – Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, Grenoble Cedex, France
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:SOFAST-HMQC Experiments for Recording Two-dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds
      description: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.
      datePublished:
      dateModified:
      pageStart:199
      pageEnd:211
      sameAs:https://doi.org/10.1007/s10858-005-4425-x
      keywords:
         Ernst angle
         fast NMR
         HMQC
         longitudinal relaxation enhancement
         protein
         residual dipolar couplings
         Biological and Medical Physics
         Biophysics
         Biochemistry
         general
         Spectroscopy/Spectrometry
      image:
      isPartOf:
         name:Journal of Biomolecular NMR
         issn:
            1573-5001
            0925-2738
         volumeNumber:33
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Kluwer Academic Publishers
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Paul Schanda
            affiliation:
                  name:UMR5075 CNRS-CEA-UJF
                  address:
                     name:Institut de Biologie Structurale – Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, Grenoble Cedex, France
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Ēriks Kupče
            affiliation:
                  name:Walton-on-Thames
                  address:
                     name:Varian Ltd., Walton-on-Thames, Surrey, United Kingdom
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Bernhard Brutscher
            affiliation:
                  name:UMR5075 CNRS-CEA-UJF
                  address:
                     name:Institut de Biologie Structurale – Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, Grenoble Cedex, France
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Journal of Biomolecular NMR
      issn:
         1573-5001
         0925-2738
      volumeNumber:33
Organization:
      name:Kluwer Academic Publishers
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:UMR5075 CNRS-CEA-UJF
      address:
         name:Institut de Biologie Structurale – Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, Grenoble Cedex, France
         type:PostalAddress
      name:Walton-on-Thames
      address:
         name:Varian Ltd., Walton-on-Thames, Surrey, United Kingdom
         type:PostalAddress
      name:UMR5075 CNRS-CEA-UJF
      address:
         name:Institut de Biologie Structurale – Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, Grenoble Cedex, France
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Paul Schanda
      affiliation:
            name:UMR5075 CNRS-CEA-UJF
            address:
               name:Institut de Biologie Structurale – Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, Grenoble Cedex, France
               type:PostalAddress
            type:Organization
      name:Ēriks Kupče
      affiliation:
            name:Walton-on-Thames
            address:
               name:Varian Ltd., Walton-on-Thames, Surrey, United Kingdom
               type:PostalAddress
            type:Organization
      name:Bernhard Brutscher
      affiliation:
            name:UMR5075 CNRS-CEA-UJF
            address:
               name:Institut de Biologie Structurale – Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, Grenoble Cedex, France
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Institut de Biologie Structurale – Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, Grenoble Cedex, France
      name:Varian Ltd., Walton-on-Thames, Surrey, United Kingdom
      name:Institut de Biologie Structurale – Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, Grenoble Cedex, France
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(76)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

3.7s.

LINK . SPRINGER . COM {}