Literature DB >> 26415

A proton NMR investigation of proline-24 cis-trans isomerism in corticotropin 1-32 and related peptides.

F Toma, S Fermandjian, M Löw, L Kisfaludy.   

Abstract

250 MHz 1H-NMR studies performed on aqueous solutions of corticotropin1-32, corticotropin1-24, corticotropin15-32, corticotropin20-32 and corticotropin15-24 have allowed the location and the subsequent assignment of the signals of Tyrosine-23 aromatic protons and valine-22 methyl protons. These signals are sensitive to the geometry of proline-24, clearly transcribe its isomerism and yield the ratio of the cis-trans conformers. It is concluded that for large peptides in specific cases, the proton signals of side chains can be used to probe the backbone conformation.

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Year:  1978        PMID: 26415     DOI: 10.1016/0005-2795(78)90481-6

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Characterization of secondary amide peptide bond isomerization: thermodynamics and kinetics from 2D NMR spectroscopy.

Authors:  Jin Zhang; Markus W Germann
Journal:  Biopolymers       Date:  2011-05-02       Impact factor: 2.505

2.  Studies of the binding and structure of adrenocorticotropin peptides in membrane mimics by NMR spectroscopy and pulsed-field gradient diffusion.

Authors:  X Gao; T C Wong
Journal:  Biophys J       Date:  1998-04       Impact factor: 4.033

  2 in total

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