title: Challenging the limit: NMR assignment of a 31 kDa helical membrane protein.
abstract: Structural determination of membrane proteins by NMR spectroscopy remains a challenge, especially for helical membrane proteins. Here we report the NMR assignment and secondary structure of a 31 kDa helical membrane protein, the C-terminal domain of Stt3p. The C-terminal domain of Stt3p has been proposed to be the catalytic domain of yeast oligosaccharyl transferase (OT), a multisubunit membrane-associated enzyme complex catalyzing N-glycosylation, which is an essential and highly conserved protein modification. NMR assignment is the first critical step in the determination of the high-resolution solution structure and further structure-function studies.
authors.affiliation: Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama 36849, USA.
authors.forename: Chengdong
authors.initials: C
authors.lastname: Huang
authors.forename: Smita
authors.initials: S
authors.lastname: Mohanty
mesh_terms: D003902:Detergents / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008823:Micelles; D008970:Molecular Weight; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013696:Temperature
chemical_list: D003902:Detergents; D008565:Membrane Proteins; D008823:Micelles