Literature DB >> 28821249

Erratum to: Charged residues next to transmembrane regions revisited: "Positive-inside rule" is complemented by the "negative inside depletion/outside enrichment rule".

James Alexander Baker1,2, Wing-Cheong Wong1, Birgit Eisenhaber1, Jim Warwicker3, Frank Eisenhaber4,5.   

Abstract

Year:  2017        PMID: 28821249      PMCID: PMC5562985          DOI: 10.1186/s12915-017-0410-6

Source DB:  PubMed          Journal:  BMC Biol        ISSN: 1741-7007            Impact factor:   7.431


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Erratum

Upon publication of the original article [1], the authors noticed that an error was introduced at proofing stage in the panel labels of Fig. 1. Instead of reading ‘a; b; c; d’, these read ‘a; b; c; c’. This has now been updated in the original article and the correct version is included in this erratum. Inconsistencies in the use of brackets around the panel labels of the figure legends have also been corrected and each panel label is now displayed in brackets. We apologise for any inconvenience caused by these errors.
Fig. 1

Negatively charged amino acids are amongst the rarest residues in TMHs and ±5 flanking residues. Bar charts of the abundance of each amino acid type in the TMHs with flank lengths of the accompanying ±5 residues from the (a) UniHuman single-pass proteins, (b) ExpAll single-pass proteins, (c) UniHuman multi-pass proteins, and (d) ExpAll multi-pass proteins. Amino acid types on the horizontal axis are listed in descending count. The bars were coloured according to categorisations of hydrophobic, neutral and hydrophilic types according to the free energy of insertion biological scale [36]. Grey represents hydrophilic amino acids that were found to have a positive ΔGapp, and blue represents hydrophobic residues with a negative ΔGapp, purple denotes negative residues and positive residues are coloured in orange. The abundances of key residues are labelled

Please see below the correct Fig. 1: Negatively charged amino acids are amongst the rarest residues in TMHs and ±5 flanking residues. Bar charts of the abundance of each amino acid type in the TMHs with flank lengths of the accompanying ±5 residues from the (a) UniHuman single-pass proteins, (b) ExpAll single-pass proteins, (c) UniHuman multi-pass proteins, and (d) ExpAll multi-pass proteins. Amino acid types on the horizontal axis are listed in descending count. The bars were coloured according to categorisations of hydrophobic, neutral and hydrophilic types according to the free energy of insertion biological scale [36]. Grey represents hydrophilic amino acids that were found to have a positive ΔGapp, and blue represents hydrophobic residues with a negative ΔGapp, purple denotes negative residues and positive residues are coloured in orange. The abundances of key residues are labelled
  1 in total

1.  Charged residues next to transmembrane regions revisited: "Positive-inside rule" is complemented by the "negative inside depletion/outside enrichment rule".

Authors:  James Alexander Baker; Wing-Cheong Wong; Birgit Eisenhaber; Jim Warwicker; Frank Eisenhaber
Journal:  BMC Biol       Date:  2017-07-24       Impact factor: 7.431

  1 in total
  1 in total

1.  Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are rationalized as ligand binding sites.

Authors:  Birgit Eisenhaber; Swati Sinha; Chaitanya K Jadalanki; Vladimir A Shitov; Qiao Wen Tan; Fernanda L Sirota; Frank Eisenhaber
Journal:  Biol Direct       Date:  2021-01-12       Impact factor: 4.540

  1 in total

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