Disulfide by Design™: a computational method for the rational design of disulfide bonds in proteins | Zendy

Alan A. Dombkowski | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Disulfide by Design™: a computational method for the rational design of disulfide bonds in proteins

Author(s) -

Alan A. Dombkowski

Publication year - 2003

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/btg231

Subject(s) - disulfide bond , protein data bank (rcsb pdb) , residue (chemistry) , computer science , amino acid residue , rational design , chemistry , bioinformatics , computational biology , biochemistry , peptide sequence , nanotechnology , materials science , biology , gene

Disulfide by Design is a program for the design of novel disulfide bonds in proteins. Protein structure files in PDB format are analyzed to identify residue pairs that are likely to form a disulfide bond if the respective amino acids are mutated to cysteines. The output displays residue pairs having the appropriate geometric characteristics for disulfide formation and provides automated generation of modified PDB files including modeled disulfides. Validation demonstrates a high level of accuracy for the algorithm.

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