title: Backbone 1H, 13C, and 15N NMR assignments of the tail domain of vinculin.
abstract: Vinculin is an essential protein involved in linking the actin cytoskeleton to sites of cell-cell and cell-matrix adhesion. Here we report the majority of the backbone 1H(N), 15N, 13C(alpha), 13CO, and side chain 13C(beta) NMR resonance assignments of the actin binding tail domain of vinculin (Vt).
authors.affiliation: Department of Biochemistry and Biophysics, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
authors.forename: Sean M
authors.initials: SM
authors.lastname: Palmer
authors.forename: Sharon L
authors.initials: SL
authors.lastname: Campbell
mesh_terms: D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons; D016596:Vinculin / Q000737:chemistry*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D016596:Vinculin