title: NMR assignment of S836: a de novo protein from a designed superfamily.
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.
authors.affiliation: Department of Chemistry, Princeton University, NJ 08544, USA.
authors.forename: Abigail
authors.initials: A
authors.lastname: Go
authors.forename: Seho
authors.initials: S
authors.lastname: Kim
authors.forename: Michael
authors.initials: M
authors.lastname: Hecht
authors.forename: Jean
authors.initials: J
authors.lastname: Baum
mesh_terms: D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D011522:Protons
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011506:Proteins; D011522:Protons