相关实验视频
Updated: Jan 9, 2026

08:43
Fused Filament Fabrication FFF of Metal-Ceramic Components
Published on: January 11, 2019
17.9K
两种FDM打印的PLA线材之间的单个关节的研究
Jaime Orellana-Barrasa1, Emilio Antón Carrasco-Otermín1, José Ygnacio Pastor1
1Centro de Investigación en Materiales Estructurales (CIME), Departamento Ciencia de Materiales, Universidad Politécnica de Madrid, 28040 Madrid, Spain.
Polymers
|December 11, 2025
概括
研究人员开发了一种新的测试来测量化沉积模型 (FDM) 关节的强度. 较高的喷嘴温度显著提高了关节强度,将故障从关节转移到发光线本身.
科学领域:
- 材料科学 材料科学 材料科学
- 添加剂制造 添加剂制造 添加剂制造
- 机械工程 机械工程
背景情况:
- 隔离和测试单个化沉积建模 (FDM) 接头的机械性能一直是一个重大挑战.
- 了解FDM关节强度对于改进模拟和预测材料性能至关重要.
研究的目的:
- 开发一种新的方法来评估单个FDM接头的表面抗拉强度 (ATS) 和断裂机制.
- 为了研究喷嘴和床温度对FDM关节层间粘合的影响.
主要方法:
- 引入十字形单关节试验 (CSJT),使用十字形样本和快速机械紧协议.
- 系统变化喷嘴 (180-215 °C) 和床 (30-120 °C) 温度,每种条件至少有12个样本.
- 故障机制的分类 (关节与导线故障) 和从拉伸测试和光学显微镜计算ATS.
主要成果:
- 关节的脱离概率在210°C喷嘴温度以上急剧下降,而ATS则在达到~50MPa的平原时增加.
- 床温度显示出更平稳的影响,脱落率下降,ATS增加.
- 喷嘴温度被确定为影响关节强度的主要因素,绘制了从关节控制到导线控制故障的过渡.
结论:
- 开发的CSJT方法提供了一种可靠,高通量和材料效率的方法来量化FDM层间粘合.
- 这些发现提供了关键数据,用于告知过程模拟和优化FDM打印参数,以提高材料强度.
相关概念视频
Studying the Cytoskeleton
8.4K
The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
8.4K
Generation of Straight or Branched Actin Filaments
3.7K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.7K
Formation of Intermediate Filaments
3.8K
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
3.8K
Disassembly of Intermediate Filaments
2.5K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.5K
Plastic Deformation in Circular Shafts
425
When materials are subjected to forces that surpass their yield strength, they undergo a process known as plastic deformation. This results in a permanent alteration or strain in their structure. This concept can be specifically applied to circular shafts, where the deformation leads to a change in its shape. The precise evaluation of this plastic deformation requires understanding the stress distribution within the circular shaft, which is achieved by calculating the maximum shearing stress in...
425
Actin Filament Depolymerization
3.7K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
In F-actin, the ADF/cofilin proteins...
3.7K

