LOGICOIL—multi-state prediction of coiled-coil oligomeric state | Zendy

Thomas L. Vincent | Zendy; Peter J. Green | Zendy; Derek N. Woolfson | Zendy

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LOGICOIL—multi-state prediction of coiled-coil oligomeric state

Author(s) -

Thomas L. Vincent,

Peter J. Green,

Derek N. Woolfson

Publication year - 2012

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/bts648

Subject(s) - coiled coil , computer science , sequence (biology) , interface (matter) , electromagnetic coil , heptad repeat , population , protein structure , oligomer , state (computer science) , computational biology , bioinformatics , peptide sequence , data mining , biology , algorithm , biophysics , chemistry , engineering , genetics , biochemistry , electrical engineering , operating system , demography , bubble , organic chemistry , maximum bubble pressure method , sociology , gene

The coiled coil is a ubiquitous α-helical protein-structure domain that directs and facilitates protein-protein interactions in a wide variety of biological processes. At the protein-sequence level, the coiled coil is readily recognized via a conspicuous heptad repeat of hydrophobic and polar residues. However, structurally coiled coils are more complicated, existing in a wide range of oligomer states and topologies. As a consequence, predicting these various states from sequence remains an unmet challenge.

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