Literature DB >> 6028395

High-resolution nuclear magnetic resonance spectroscopy. Advances in instrumentation in this field are leading to new applications in chemistry and biology.

R C Ferguson, W D Phillips.   

Abstract

The rapid development of NMR spectroscopy has been characterized by a succession of discrete, significant advances in instrumentation, as well as by less dramatic but cumulatively important improvements in instrument performance, experimental techniques, spectral analysis, and theory. Most significant are the advances in magnet technology, which within 13 years increased the available field strengths from 7.04 to 51.7 kilogauss (with corresponding increase in the PMR frequency from 30 to 220 megahertz). Great improvements in spectrometer stability and in the coupling of spectrometers with on-line computers have so improved sensitivity that some nuclei possessing less favorable NMR characteristics can now be studied.

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Year:  1967        PMID: 6028395     DOI: 10.1126/science.157.3786.257

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  3 in total

Review 1.  Mass Spectrometry Methods for Measuring Protein Stability.

Authors:  Daniel D Vallejo; Carolina Rojas Ramírez; Kristine F Parson; Yilin Han; Varun V Gadkari; Brandon T Ruotolo
Journal:  Chem Rev       Date:  2022-03-22       Impact factor: 72.087

2.  The reaction of an iridium PNP complex with parahydrogen facilitates polarisation transfer without chemical change.

Authors:  Arthur J Holmes; Peter J Rayner; Michael J Cowley; Gary G R Green; Adrian C Whitwood; Simon B Duckett
Journal:  Dalton Trans       Date:  2015-01-21       Impact factor: 4.390

3.  Monitoring protein unfolding transitions by NMR-spectroscopy.

Authors:  Matthias Dreydoppel; Jochen Balbach; Ulrich Weininger
Journal:  J Biomol NMR       Date:  2022-01-04       Impact factor: 2.582

  3 in total

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