Two novel three-dimensional coordination polymers with [Ag(CN)2]− as bridging ligands: synthesis and structural characterization of {KMn[Ag(CN)2]3(H2O) }n and {Mn[Ag(CN)2]2(bpy)2}n (bpy=4,4′-bipyridine)

2003 ◽  
Vol 6 (7) ◽  
pp. 873-876 ◽  
Author(s):  
Wen Dong ◽  
Qing-Lun Wang ◽  
Shu-Feng Si ◽  
Dai-Zheng Liao ◽  
Zong-Hui Jiang ◽  
...  
Keyword(s):  
Coordination Polymers ◽  
Structural Characterization ◽  
Three Dimensional ◽  
Bridging Ligands

Synthesis and structural characterization of homochiral coordination polymers with imidazole-based monocarboxylate ligands

2019 ◽  
Vol 48 (24) ◽  
pp. 8731-8739 ◽  
Author(s):  
Elena Borrego ◽  
Antonio I. Nicasio ◽  
Eleuterio Álvarez ◽  
Francisco Montilla ◽  
José Manuel Córdoba ◽  
...  
Keyword(s):  
Coordination Polymers ◽  
Structural Characterization ◽  
Two Dimensional ◽  
Bridging Ligands ◽  
Silver Copper ◽  
Copper And Zinc

Two-dimensional homochiral coordination polymers of sodium, silver, copper and zinc were obtained with 2alkyl,2-(1H-imidazol-1-yl)acetate anions as bridging ligands.

Design, synthesis, and three-dimensional structural characterization of a constrained Ω-loop excised from interleukin-1α

Tetrahedron ◽  
1993 ◽  
Vol 49 (17) ◽  
pp. 3629-3640 ◽  
Author(s):  
Ramakanth Sarabu ◽  
Kathleen Lovey ◽  
Vincent S. Madison ◽  
David C. Fry ◽  
David N. Greeley ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Three Dimensional ◽  
Design Synthesis ◽  
Interleukin 1Α

scholarly journals Synthesis and structural characterization of hexa-μ2-chlorido-μ4-oxido-tetrakis{[4-(phenylethynyl)pyridine-κN]copper(II)} dichloromethane monosolvate

2021 ◽  
Vol 77 (1) ◽  
pp. 42-46
Author(s):  
Rayya A. Al Balushi ◽  
Muhammad S. Khan ◽  
Md. Serajul Haque Faizi ◽  
Ashanul Haque ◽  
Kieran Molloy ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Crystal Structure ◽  
Structural Characterization ◽  
Title Compound ◽  
Three Dimensional ◽  
Hirshfeld Surface ◽  
The Core ◽  
Dimensional Network ◽  
Packing Arrangement

In the crystal structure of the title compound, [Cu4Cl6O(C13H9N)4]·CH2Cl2, the core molecular structure consists of a Cu4 tetrahedron with a central interstitial O atom. Each edge of the Cu4 tetrahedron is bridged by a chlorido ligand. Each copper(II) cation is coordinated to the central O atom, two chlorido ligands and one N atom of the 4-phenylethynylpyridine ligand. In the crystal, the molecules are linked by intermolecular C—H...Cl interactions. Furthermore, C—H...π and π–π interactions also connect the molecules, forming a three-dimensional network. Hirshfeld surface analysis indicates that the most important contributions for the packing arrangement are from H...H and C...H/H...C interactions.

Structural Characterization of Linear Three-Dimensional Random Chains: Energetic Behaviour and Anisotropy

2021 ◽  
pp. 179-191
Author(s):  
David R. Avellaneda B. ◽  
Ramón E. R. González ◽  
Paola Ariza-Colpas ◽  
Roberto Cesar Morales-Ortega ◽  
Carlos Andrés Collazos-Morales
Keyword(s):  
Structural Characterization ◽  
Three Dimensional

scholarly journals Structural Basis for Env Incorporation into HIV-1 Particles

Proceedings ◽  
2020 ◽  
Vol 50 (1) ◽  
pp. 114
Author(s):  
R. Elliot Murphy ◽  
Alexandra B. Samal ◽  
Gunnar Eastep ◽  
Ruba H. Ghanam ◽  
Peter E. Prevelige ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Late Phase ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Membrane Interactions ◽  
Env Protein ◽  
Gag Assembly ◽  
Hiv 1

During the late phase of the HIV-1 replication cycle, the Gag polyproteins are transported to the plasma membrane (PM) for assembly. Gag targeting and assembly on the PM is dependent on interactions between its matrix (MA) domain and phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2). Subsequent to Gag assembly, the envelope (Env) protein is recruited to the PM for incorporation into virus particles. Evidence suggests that the incorporation of the Env protein is mediated by interactions between the MA domain of Gag and the cytoplasmic tail of the gp41 subunit of Env (gp41CT), a mechanism that remains to be elucidated. Trimerization of the MA domain of Gag appears to be an obligatory step for this interaction. The interplay between gp41CT, the MA trimer, and the membrane has yet to be determined. Our lab has pioneered methods and approaches to investigate, at the molecular level, how the retroviral MA domains of Gag interact with membranes, a key requirement for understanding the Gag assembly and Env incorporation. Herein, we devised innovative approaches that will enable the structural characterization of the gp41CT–MA–membrane interactions. We employed structural biology (NMR and cryo-electron microscopy, biophysical methods, and biochemical tools to generate a macromolecular picture of how the MA domain of Gag binds to the membrane and how it interacts with gp41CT. To this end, we: (i) determined the three-dimensional structure of HIV-1 gp41CT and characterized its interaction with the membrane, (ii) engineered trimeric constructs of gp41CT and the MA to recapitulate the native and functional states of the proteins, and (iii) utilized membrane nanodisc technology to anchor the MA and gp41CT proteins. Our studies will allow for a detailed structural characterization of the gp41CT–MA–membrane interactions, which will advance our knowledge of HIV-1 Gag assembly and Env incorporation.

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