Literature DB >> 11449562

[Left-handed helix conformation of poly-L-proline II type in globular proteins. Statistics of incidence and a role of sequence].

P K Vlasov1, G T Kilosanidze, D L Ukrainskiĭ, A V Kuz'min, V G Tumanian, N G Esipova.   

Abstract

Regions of left-handed polyproline II type conformation in globular proteins were studied throughout the PDB bank. The length and sequence of corresponding fragments were analyzed. It was found that a lot of tetrapeptides (from combinatorial possible ones) show the tendency to be included in the left-handed helices. Much more tetrapeptides do not occur in this structure type.

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Year:  2001        PMID: 11449562

Source DB:  PubMed          Journal:  Biofizika        ISSN: 0006-3029


  2 in total

1.  Empirical isotropic chemical shift surfaces.

Authors:  Eszter Czinki; Attila G Császár
Journal:  J Biomol NMR       Date:  2007-06-26       Impact factor: 2.835

2.  Assignment of PolyProline II conformation and analysis of sequence--structure relationship.

Authors:  Yohann Mansiaux; Agnel Praveen Joseph; Jean-Christophe Gelly; Alexandre G de Brevern
Journal:  PLoS One       Date:  2011-03-31       Impact factor: 3.240

  2 in total

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