Literature DB >> 903527

Peptide hydrogen bonding. Conformation dependence of the carbonyl carbon-13 nuclear magnetic resonance chemical shifts in ferrichrome. A study by 13C-[15N] Fourier double resonance spectroscopy1a.

M Llinás, D M Wilson, M P Klein.   

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Year:  1977        PMID： 903527     DOI： 10.1021/ja00463a010

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


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  3 in total

1.  An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins.

Authors:  A Bax; M Ikura
Journal:  J Biomol NMR       Date:  1991-05       Impact factor: 2.835

2.  Amide proton spin-lattice relaxation in polypeptides. A field-dependence study of the proton and nitrogen dipolar interactions in alumichrome.

Authors:  M Llinás; M P Klein; K Wüthrich
Journal:  Biophys J       Date:  1978-12       Impact factor: 4.033

3.  Peptaibol zervamicin IIb structure and dynamics refinement from transhydrogen bond J couplings.

Authors:  Z O Shenkarev; T A Balashova; Z A Yakimenko; T V Ovchinnikova; A S Arseniev
Journal:  Biophys J       Date:  2004-06       Impact factor: 4.033
  3 in total

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