Literature DB >> 12713961

High-sensitivity sapphire cells for high pressure NMR spectroscopy on proteins.

Martin Reinhard Arnold1, Hans Robert Kalbitzer, Werner Kremer.   

Abstract

High pressure NMR spectroscopy is a most exciting method for studying the structural anisotropy and conformational dynamics of proteins. The restricted volume of the high pressure glass cells causes a poor signal to noise ratio which up to now renders the application of most of the multidimensional NMR experiments impossible. The method presented here using high strength single crystal sapphire cells doubles the signal-to-noise ratio and allows to perform high pressure NMR measurements more easily. As a first application the difference of partial molar volumes caused by cis-trans-isomerisation of a prolyl peptide bond in the tetrapeptide Gly-Gly-Pro-Ala could be determined as 0.25 ml mol(-1) at 305 K.

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Year:  2003        PMID: 12713961     DOI: 10.1016/s1090-7807(02)00179-9

Source DB:  PubMed          Journal:  J Magn Reson        ISSN: 1090-7807            Impact factor:   2.229


  8 in total

1.  Coupled motion in proteins revealed by pressure perturbation.

Authors:  Yinan Fu; Vignesh Kasinath; Veronica R Moorman; Nathaniel V Nucci; Vincent J Hilser; A Joshua Wand
Journal:  J Am Chem Soc       Date:  2012-04-10       Impact factor: 15.419

2.  Infrequent cavity-forming fluctuations in HPr from Staphylococcus carnosus revealed by pressure- and temperature-dependent tyrosine ring flips.

Authors:  Mineyuki Hattori; Hua Li; Hiroaki Yamada; Kazuyuki Akasaka; Wolfgang Hengstenberg; Wolfram Gronwald; Hans Robert Kalbitzer
Journal:  Protein Sci       Date:  2004-12       Impact factor: 6.725

3.  Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.

Authors:  José A Caro; A Joshua Wand
Journal:  Methods       Date:  2018-06-30       Impact factor: 3.608

4.  Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy.

Authors:  Norman Kachel; Werner Kremer; Ralph Zahn; Hans Robert Kalbitzer
Journal:  BMC Struct Biol       Date:  2006-07-17

5.  Magnetic flux tailoring through Lenz lenses for ultrasmall samples: A new pathway to high-pressure nuclear magnetic resonance.

Authors:  Thomas Meier; Nan Wang; Dario Mager; Jan G Korvink; Sylvain Petitgirard; Leonid Dubrovinsky
Journal:  Sci Adv       Date:  2017-12-08       Impact factor: 14.136

Review 6.  Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways.

Authors:  Cécile Dubois; Isaline Herrada; Philippe Barthe; Christian Roumestand
Journal:  Molecules       Date:  2020-11-26       Impact factor: 4.411

7.  A miniaturized spectrometer for NMR relaxometry under extreme conditions.

Authors:  Yiqiao Tang; David McCowan; Yi-Qiao Song
Journal:  Sci Rep       Date:  2019-08-01       Impact factor: 4.379

8.  Refolding of Cold-Denatured Barstar Induced by Radio-Frequency Heating: A New Method to Study Protein Folding by Real-Time NMR Spectroscopy.

Authors:  György Pintér; Harald Schwalbe
Journal:  Angew Chem Int Ed Engl       Date:  2020-09-25       Impact factor: 15.336

  8 in total

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