Protein backbone ensemble generation explores the local structural space of unseen natural homologs | Zendy

Christian D. Schenkelberg | Zendy; Christopher Bystroff | Zendy

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Protein backbone ensemble generation explores the local structural space of unseen natural homologs

Author(s) -

Christian D. Schenkelberg,

Christopher Bystroff

Publication year - 2016

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/btw001

Subject(s) - protein superfamily , sequence (biology) , computer science , protein design , function (biology) , protein structure , position (finance) , sequence alignment , algorithm , computational biology , peptide sequence , biology , genetics , biochemistry , finance , gene , economics

Mutations in homologous proteins affect changes in the backbone conformation that involve a complex interplay of forces which are difficult to predict. Protein design algorithms need to anticipate these backbone changes in order to accurately calculate the energy of the structure given an amino acid sequence, without knowledge of the final, designed sequence. This is related to the problem of predicting small changes in the backbone between highly similar sequences.

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