Literature DB >> 22148627

Disentangling crystallographic inequivalence and crystallographic forms of L-arginine by one- and two-dimensional solid-state NMR spectroscopy.

Jose-Enrique Herbert-Pucheta1, Henri Colaux, Geoffrey Bodenhausen, Piotr Tekely.   

Abstract

Overlapping (13)C or (15)N solid-state NMR spectra from crystallographically different forms of L-arginine hydrochloride can be separated by exploiting differential proton T(1) relaxation in conjunction with cross-polarization. Dipolar (13)C-(13)C and (15)N-(15)N two-dimensional correlation experiments reveal resonances belonging to crystallographically and magnetically inequivalent molecules.
© 2011 American Chemical Society

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Year:  2011        PMID: 22148627     DOI: 10.1021/jp209644k

Source DB:  PubMed          Journal:  J Phys Chem B        ISSN: 1520-5207            Impact factor:   2.991


  1 in total

1.  Quantitative one- and two-dimensional 13C spectra of microcrystalline proteins with enhanced intensity.

Authors:  Rudra N Purusottam; Geoffrey Bodenhausen; Piotr Tekely
Journal:  J Biomol NMR       Date:  2013-06-29       Impact factor: 2.835

  1 in total

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