Valence band offset of InN/AlN heterojunctions measured by X-ray photoelectron spectroscopy

The valence band offset of wurtzite-InN/AlN (0001) heterojunctions is determined by x-ray photoelectron spectroscopy to be 1.52±0.17 eV. Together with the resulting conduction band offset of 4.0±0.2 eV, a type-I heterojunction forms between InN and AlN in the straddling arrangement

Surface electronic properties of undoped InAlN alloys

The variation in surface electronic properties of undoped c-plane InxAl1−xN alloys has been investigated across the composition range using a combination of high-resolution x-ray photoemission spectroscopy and single-field Hall effect measurements. For the In-rich alloys, electron accumulation layers, accompanied by a downward band bending, are present at the surface, with a decrease to approximately flatband conditions with increasing Al composition. However, for the Al-rich alloys, the undoped samples were found to be insulating with approximate midgap pinning of the surface Fermi level observed

A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain

Factor XI (FXI) is the zymogen of FXIa, which cleaves FIX in the intrinsic pathway of coagulation. FXI is known to exist as a dimer and interacts with multiple proteins via its 4 apple domains in the “saucer section” of the enzyme; however, to date, no complex crystal structure has been described. To investigate protein interactions of FXI, a large random peptide library consisting of 106 to 107 peptides was screened for FXI binding, which identified a series of FXI binding motifs containing the signature Asp-Phe-Pro (DFP) tripeptide. Motifs containing this core tripeptide were found in diverse proteins, including the known ligand high-molecular-weight kininogen (HK), as well as the extracellular matrix proteins laminin and collagen V. To define the binding site on FXI, we determined the crystal structure of FXI in complex with the HK-derived peptide NPISDFPDT. This revealed the location of the DFP peptide bound to the FXI apple 2 domain, and central to the interaction, the DFP phenylalanine side-chain inserts into a major hydrophobic pocket in the apple 2 domain and the isoleucine occupies a flanking minor pocket. Two further structures of FXI in complex with the laminin-derived peptide EFPDFP and a DFP peptide from the random screen demonstrated binding in the same pocket, although in a slightly different conformation, thus revealing some flexibility in the molecular interactions of the FXI apple 2 domain. (Blood. 2016;00(00):1-9