Crystal structure of 2-(2-naphthyl)-4,6-dimethylpyrimidine, C(16)H(14)N(2)

C(16)H(14)N(2), monoclinic, P12(1)/c1 (no. 14), a = 8.387(1) angstrom, b = 17.453(3) angstrom, c = 8.694(1) angstrom, beta = 93.092(2)degrees, V = 1270.8 angstrom(3), Z = 4, R(gt)(F) = 0.046, wR(ref)(F(2)) = 0.129, T = 294 K.program for innovation of science and technology talents of Henan Province[104200510022]; program for science and technology leaders of Zhengzhou City[10LJRC174]; Doctor Foundation[D09004]; program for innovative research team of Henan Institute of Engineering[2009IRTHNIE05

Study on open science: The general state of the play in Open Science principles and practices at European life sciences institutes

Nowadays, open science is a hot topic on all levels and also is one of the priorities of the European Research Area. Components that are commonly associated with open science are open access, open data, open methodology, open source, open peer review, open science policies and citizen science. Open science may a great potential to connect and influence the practices of researchers, funding institutions and the public. In this paper, we evaluate the level of openness based on public surveys at four European life sciences institute

Comparison of Non-covalent Interactions Between a Series of N-Phosphoryl Dipeptide or Methyl Esters and Protein by Electrospray Ionization Mass Spectrometry

The non-covalent interaction between a series of N-phosphoryl dipeptides (or methyl esters) (DPP) and protein was studied by ESI-MS and UV-vis spectrometer. The function of different groups in DPP and binding sites of protein were investigated. The results revealed that hydroxyl and aromatic ring in DPP were both important group for the interaction, and aromatic ring had double functions on the interaction. In addition, the molecular size, flexibility and steric hindrance showed obvious effects on the interaction, while, the chirality, sequence and length of carbon chains (changing 1-2C) of amino acid residue in DPP showed little effects on the interaction under the experimental conditions. Phosphoryl oligopeptides having extended structure, good molecular flexibility and smaller spatial hindrance could contract the protein conformation in solution. The aromatic, basic, acid and amide amino acid residues of protein may be the main binding sites and contributed to the survival of the complexes.National Natural Science Foundation of China[20572016, 20672104, 20772023]; Doctor Foundation[D09004]; program for the innovative research team of Henan Institute of Engineering[2009IRTHNIE05]; Zhengzhou Universit