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1.
The isomerization of poly-L -proline in different solvents has been studied by NMR spectroscopy. Different resonance signals for the CHα protons have been obtained for the two different helical conformations of thus compound, namely form I and form II. 相似文献
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G Esposito S Cauci F Fogolari E Alessio M Scocchi F Quadrifoglio P Viglino 《Biochemistry》1992,31(31):7094-7103
The reaction between the antitumor octahedral complex trans-RuCl2(DMSO)4 and d(GpG) leads to the formation of a stable compound characterized by a covalent bifunctional coordination of the bases to the metal center. The structure of the compound has been fully characterized by NMR and molecular modeling studies, showing the presence of two N7-coordinated guanine moieties in a head to head conformation, two dimethyl sulfoxide molecules, and one halogen atom in the coordination sphere of the ruthenium. The glycosidic chi angles are essentially in the anti range, the sugar puckering of the 5'G is 3'-endo (100% N), whereas that of the 3'G is more flexible but mainly in 2'-endo conformation (85% S), the two bases are strongly destacked. The compound shows structural features which are surprisingly similar to those exhibited by the corresponding cisplatin complex, indicating that such a way of interaction with DNA is not exclusive to Pt or to metals with square planar coordination geometries. 相似文献
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The reaction of the antitumor octahedral complex trans-RuCl2(DMSO)4 with 2'deoxyguanosine leads to the reversible formation of two diastereoisomeric monoadducts and one biadduct. This shows that it is possible to accommodate two purine bases in a cis configuration in an octahedral transition metal complex which exhibits antiblastic activity. All the product compounds are characterized by a guanine moiety coordination via the N7 atom. A marked decrease (about two pK units) is observed for the N1H pKa of the coordinated guanine moieties. The reversibility of the monodentate binding could explain the low toxicity of the ruthenium(II) complexes. 相似文献
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Frantz Alain C. Viglino Andrea Wilwert Elodie Cruz Ana-Paula Wittische Julian Weigand Alexander M. Buijk Jacky Nyssen Pierrette Dekeukeleire Daan Dekker Jasja J.A. Horsburgh Gavin J. Schneider Simone Lang Mara Caniglia Romolo Galaverni Marco Schleimer Anna Bücs Szilárd-Lehel Pir Jacques B. 《Biodiversity and Conservation》2022,31(3):925-948
Biodiversity and Conservation - In the European Union, all bat species are strictly protected and member states must ensure their conservation. However, if populations are genetically structured,... 相似文献
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Rosano C Zuccotti S Mangione P Giorgetti S Bellotti V Pettirossi F Corazza A Viglino P Esposito G Bolognesi M 《Journal of molecular biology》2004,335(4):1051-1064
beta2-Microglobulin (beta2m) is the non-covalently bound light chain of the human class I major histocompatibility complex (MHC-I). The natural turnover of MHC-I gives rise to the release of beta2m into plasmatic fluids and to its catabolism in the kidney. beta2m dissociation from the heavy chain of the complex is a severe complication in patients receiving prolonged hemodialysis. As a consequence of renal failure, the increasing beta2m concentrations can lead to deposition of the protein as amyloid fibrils. Here we characterize the His31-->Tyr human beta2m mutant, a non-natural form of beta2m that is more stable than the wild-type protein, displaying a ten-fold acceleration of the slow phase of folding. We report the 2.9A resolution crystal structure and the NMR characterization of the mutant beta2m, focussing on selected structural features and on the molecular packing observed in the crystals. Juxtaposition of the four mutant beta2m molecules contained in the crystal asymmetric unit, and specific hydrogen bonds, stabilize a compact protein assembly. Conformational heterogeneity of the four independent molecules, some of their mutual interactions and partial unpairing of the N-terminal beta-strand in one protomer are in keeping with the amyloidogenic properties displayed by the mutant beta2m. 相似文献
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Pagano K Ramazzotti M Viglino P Esposito G Degl'Innocenti D Taddei N Corazza A 《Journal of biomolecular NMR》2006,36(3):199-204
The solution structure of Escherichia coli acylphosphatase (E. coli AcP), a small enzyme catalyzing the hydrolysis of acylphosphates, was determined by (1)H and (15)N NMR and restrained modelling calculation. In analogy with the other members of AcP family, E. coli AcP shows an alpha/beta sandwich domain composed of four antiparallel and one parallel beta-strand, assembled in a five-stranded beta-sheet facing two antiparallel alpha-helices. The pairwise RMSD values calculated for the backbone atoms of E. coli and Sulfolobus solfataricus AcP, Bovine common type AcP and Horse muscle AcP are 2.18, 5.31 and 5.12 A, respectively. No significant differences are present in the active site region and the catalytic residue side chains are consistently positioned in the structures. 相似文献
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