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We study the formation of the charge-density wave long-range order in a system of repulsive 1D electrons coupled to 3D phonons. We show that the charge-density wave can be stabilized by interaction with phonons in quasi-1D crystals and semiconducting nanowires. In the case of metallic atomic chains, interaction with phonons of a 3D substrate is not enough, and violation of the translational invariance by commensurable perturbation or disorder is needed. The possibility of stabilization of superconductivity in 1D electrons with attraction by means of tunnel coupling to a 3D metal is considered. 相似文献
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V.E. Kuz’min A.G. Artemenko S.Yu. Makan S.A. Andronati 《SAR and QSAR in environmental research》2013,24(3-4):213-244
The influence of molecular structure of 346 ligands on their affinity for 5-HT1A receptors was investigated. It was shown that the effectiveness of the proposed novel approach for interpretation of decision tree models compared favourably with the PLS method. In the context of the proposed approach, molecular fragments and their values of the relative influence on the affinity for 5-HT1A receptors were defined. 相似文献
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Tatiana Y. Samgina Egor A. Vorontsov Vladimir A. Gorshkov Konstantin A. Artemenko Roman A. Zubarev Jimmy A. Ytterberg Albert T. Lebedev 《Journal of the American Society for Mass Spectrometry》2013,24(7):1037-1044
Collision-induced dissociation (CID) spectra of long non-tryptic peptides are usually quite complicated and rather difficult to interpret. Disulfide bond formed by two cysteine residues at C-terminus of frog skin peptides precludes one to determine sequence inside the forming loop. Thereby, chemical modification of S–S bonds is often used in “bottom up” sequencing approach. However, low-energy CID spectra of natural non-tryptic peptides with C-terminal disulfide cycle demonstrate an unusual fragmentation route, which may be used to elucidate the “hidden” C-terminal sequence. Low charge state protonated molecules experience peptide bond cleavage at the N-terminus of C-terminal cysteine. The forming isomeric acyclic ions serve as precursors for a series of b-type ions revealing sequence inside former disulfide cycle. The reaction is preferable for peptides with basic lysine residues inside the cycle. It may also be activated by acidic protons of Asp and Glu residues neighboring the loop. The observed cleavages may be quite competitive, revealing the sequence inside disulfide cycle, although S–S bond rupture does not occur in this case. Figure
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