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Charged single alpha-helices in proteomes revealed by a consensus prediction approach

  • Published:2012-04 Issue:4 Volume:1824 Page:637-646
  • ISSN:1570-9639
  • Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
  • language:en
  • Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Gáspári Zoltán,Süveges Dániel,Perczel András,Nyitray László,Tóth Gábor

Funder

Hungarian Scientific Research Fund

International Centre for Genetic Engineering and Biotechnology

European Union

European Social Fund

János Bolyai Research Fellowship

Ferenc Deák Fellowship

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference25 articles.

1. Dynamic charge interactions create surprising rigidity in the ER/K α-helical protein motif;Sivaramakrishnan;Proc. Natl. Acad. Sci. U. S. A.,2008

2. Charged single α-helix: a versatile protein structural motif;Süveges;Proteins,2009

3. When a predicted coiled coil is really a single α-helix, in myosins and other proteins;Peckham;Soft Matter,2009

4. Role of catioinc residues in fine tuning the flexibiliy of charged single α-helices;Espinoza-Fonseca;Biophys. J.,2009

5. Myosin VI: an innovative motor that challenged the swing lever arm hypothesis;Spudich;Nat. Rev. Mol. Cell Biol.,2010
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