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

Abigail Go; Seho Kim; Michael Hecht; Jean Baum

doi:10.1007/s12104-007-9059-3

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

Abigail Go, Seho Kim, Michael Hecht, Jean Baum

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	213-215
Number of pages	3
Journal	Biomolecular NMR Assignments
Volume	1
Issue number	2
DOIs	https://doi.org/10.1007/s12104-007-9059-3
State	Published - 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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10.1007/s12104-007-9059-3

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AU - Hecht, Michael

AU - Baum, Jean

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KW - Binary patterning

KW - De novo proteins

KW - Four-helix bundle

KW - NMR assignments

KW - Protein design

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

Abstract

All Science Journal Classification (ASJC) codes

Keywords

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