Correlated mutations select misfolded from properly folded proteins | Zendy

Paweł Woźniak | Zendy; Gert Vriend | Zendy; Małgorzata Kotulska | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Correlated mutations select misfolded from properly folded proteins

Author(s) -

Paweł Woźniak,

Gert Vriend,

Małgorzata Kotulska

Publication year - 2017

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/btx013

Subject(s) - decoy , protein data bank (rcsb pdb) , computer science , computational biology , casp , protein folding , protein structure , protein structure prediction , sequence (biology) , data mining , algorithm , bioinformatics , chemistry , biology , biochemistry , receptor

The recently developed direct coupling analysis (DCA) method has greatly improved the accuracy with which residue-residue contacts can be predicted from multiple sequence alignments. Contact prediction accuracy, though, is still often not sufficient for complete ab initio protein structure prediction. DCA can, however, support protein structure studies in several ways.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research