NMR assignment of S836: A de novo protein from a designed superfamily

Abigail Go, Seho Kim, Michael Hecht, Jean Baum

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Libraries of de novo proteins provide an opportunity to explore the structural potential of biological macromolecules that have not been biased by billions of years of evolutionary selection. Characterization of individual members of such libraries provides insight into the diversity of structure and dynamics accessible to nascent protein superfamilies in the absence of evolutionary optimization. Here we report the backbone and side chain chemical shifts of protein S836 from a superfamily of designed 4-helix bundles.

Original languageEnglish (US)
Pages (from-to)213-215
Number of pages3
JournalBiomolecular NMR Assignments
Volume1
Issue number2
DOIs
StatePublished - Dec 2007

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

Keywords

  • Alpha helix
  • Binary patterning
  • De novo proteins
  • Four-helix bundle
  • NMR assignments
  • Protein design

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