Literature DB >> 1993078

Structural flexibility of Aib-containing peptides: the N-terminal tripeptide of trichotoxin.

R Gessmann1, H Brueckner, M Kokkinidis.   

Abstract

The sequence Aib-Gly-Aib which corresponds to the N-terminus of the microheterogeneous peptide antibiotic trichotoxin has been studied crystallographically in the context of different protecting groups. Peptides Ac-Aib-Gly-Aib-OH (A) and Z-Aib-Gly-Aib-OH (B) form beta-turns. Both peptides show a remarkable conformational flexibility forming a large variety of beta-turns of different types.

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Year:  1991        PMID: 1993078     DOI: 10.1016/0006-291x(91)91499-3

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  Heterogeneous-Backbone Foldamer Mimics of a Computationally Designed, Disulfide-Rich Miniprotein.

Authors:  Chino C Cabalteja; Daniel S Mihalko; W Seth Horne
Journal:  Chembiochem       Date:  2018-11-27       Impact factor: 3.164

2.  Use ofα-aminoisobutyric acid and isovaline as marker amino acids for the detection of fungal polypeptide antibiotics. Screening ofHypocrea.

Authors:  H Brückner; J Maisch; C Reinecke; A Kimonyo
Journal:  Amino Acids       Date:  1991-06       Impact factor: 3.520

3.  Crystal structures of Z-Gly-Aib-O-·0.5Ca2+·H2O and Z-Gly-Aib-OH.

Authors:  Renate Gessmann; Hans Brückner; Kyriacos Petratos
Journal:  Acta Crystallogr E Crystallogr Commun       Date:  2018-07-27
  3 in total

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