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Vasudevan Lakshminarayanan Cindhuja Chockalingam Dr. Eduardo Mendes Dr. Prof. Jan H. van Esch 《Chemphyschem》2021,22(21):2256-2261
Properties such as shear modulus, gelation time, structure of supramolecular hydrogels are strongly dependent on self-assembly, gelation triggering mechanism and processes used to form the gel. In our work we extend reported rheology analysis methodologies to pH-triggered supramolecular gels to understand structural insight using a model system based on N−N’ Dibenzoyl-L-Cystine pH-triggered hydrogelator and Glucono-δ-Lactone as the trigger. We observed that Avrami growth model when applied to time-sweep rheological data of gels formed at lower trigger concentrations provide estimates of fractal dimension which agree well compared with visualization of the microstructure as seen via Confocal Laser Scanning Microscopy, for a range of gelator concentrations. 相似文献
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Spatially Resolved Confocal Resonant Raman Microscopic Analysis of Anode‐Grown Geobacter sulfurreducens Biofilms 下载免费PDF全文
When grown on the surface of an anode electrode, Geobacter sulfurreducens forms a multi‐cell thick biofilm in which all cells appear to couple the oxidation of acetate with electron transport to the anode, which serves as the terminal metabolic electron acceptor. Just how electrons are transported through such a biofilm from cells to the underlying anode surface over distances that can exceed 20 microns remains unresolved. Current evidence suggests it may occur by electron hopping through a proposed network of redox cofactors composed of immobile outer membrane and/or extracellular multi‐heme c‐type cytochromes. In the present work, we perform a spatially resolved confocal resonant Raman (CRR) microscopic analysis to investigate anode‐grown Geobacter biofilms. The results confirm the presence of an intra‐biofilm redox gradient whereby the probability that a heme is in the reduced state increases with increasing distance from the anode surface. Such a gradient is required to drive electron transport toward the anode surface by electron hopping via cytochromes. The results also indicate that at open circuit, when electrons are expected to accumulate in redox cofactors involved in electron transport due to the inability of the anode to accept electrons, nearly all c‐type cytochrome hemes detected in the biofilm are oxidized. The same outcome occurs when a comparable potential to that measured at open circuit (?0.30 V vs. SHE) is applied to the anode, whereas nearly all hemes are reduced when an exceedingly negative potential (?0.50 V vs. SHE) is applied to the anode. These results suggest that nearly all c‐type cytochrome hemes detected in the biofilm can be electrochemically accessed by the electrode, but most have oxidation potentials too negative to transport electrons originating from acetate metabolism. The results also reveal a lateral heterogeneity (x–y dimensions) in the type of c‐type cytochromes within the biofilm that may affect electron transport to the electrode. 相似文献
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Distinct Spatial Relationship of the Interleukin‐9 Receptor with Interleukin‐2 Receptor and Major Histocompatibility Complex Glycoproteins in Human T Lymphoma Cells 下载免费PDF全文
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新型显微成像光谱仪系统中线阵针孔离焦研究 总被引:1,自引:0,他引:1
显微成像光谱仪技术是最近新兴的一种生物组织检测方法,它可以广泛应用在生物医学检测,疑难病症分析、预防、诊断中,已经成为当今生物组织检测领域研究的热点。提出了一种新型的基于线阵针孔阵列的激光扫描共焦显微成像光谱仪系统LP-LSCMIS方案,介绍了其工作原理及优点,讨论了该装置中线阵针孔阵列离焦对系统性能的影响,分析了离焦对生物组织荧光图像的光谱分辨和自体荧光光谱的调制深度的影响。推导出了光谱分辨和调制深度与离焦量的关系式。结果表明,离焦对仪器的性能有较大的影响,因此在装置装调时要求有更高精度的调整机构。 相似文献
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为了克服太空环境的复杂性,满足航天工程的空间使用要求,研制一款2 500万像素宽光谱共焦成像的微型星载相机光学系统。该系统适应卫星发射和在轨道运行的恶劣环境,具有抗冲击震动、耐太空高温差强辐射,体积小,质量轻等优点。设计的系统可在450 nm~800 nm的谱段内清晰成像,焦距181 mm,入瞳口径45 mm,视场角10.4°,边缘相对照度0.81,轴上点MTF:0.57@55 lp/mm,0.33@110 lp/mm,畸变1.2%,镜头质量622 g,外形尺寸Φ58.3 mm×117 mm,抗辐照性能≥5 krad。通过温度适应性的模拟和优化,用户进行?30 ℃~+70 ℃光学镜头热真空试验,可正常工作。该系统已成功应用于天宫二号伴飞卫星相机中,获得的图像清晰稳定,为空间遥感实验观测发挥了重要的作用。 相似文献
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The immobilization of trypsin on porous glycidyl methacrylate (GMA–GDMA) beads has been investigated. In particular, the distribution within the beads of trypsin and of dextran used for hydrophilizing the bead surface prior to protein immobilization was investigated with confocal microscopy. For the system investigated, the fluorescence intensity profiles obtained when using borate buffer as an ambient solution displayed a distinct minimum at the center of the beads, irrespective of the observation depth. However, by reduction of the refractive index difference between the solution and the beads through the addition of glucose to the aqueous solution, artifacts relating to optical length differences could be reduced. For both low molecular weight fluorescein isothiocyanate (FITC), FITC-labeled trypsin, and FITC-labeled dextran, an essentially homogeneous distribution throughout the beads was observed. This simple “contrast matching” method seems therefore to be an interesting tool when investigating the distribution of immobilized protein in porous chromatography media. 相似文献
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