A Chain-Based 2 D Cobalt(II) Coordination Polymer with a “Crab-Like” Flexible Dicarboxylate Ligand: A Weak Ferromagnetic Single-Chain Magnet

2013 ◽  
Vol 8 (9) ◽  
pp. 1985-1989 ◽  
Author(s):  
Qingfu Zhang ◽  
Haina Zhang ◽  
Suyuan Zeng ◽  
Dezhi Sun ◽  
Chong Zhang
Keyword(s):  
Coordination Polymer ◽  
Single Chain ◽  
Dicarboxylate Ligand ◽  
A Chain ◽  
Weak Ferromagnetic

LIPOPOLYSACCHARIDE-SENSITIVE SERINE-PROTEASE ZYMOGEN (FACTOR C) OF LIMULUS HEMOCYTES: IDENTIFICATION AND ALIGNMENT OF PROTEOLYTIC FRAGMENTS PRODUCED DURING THE ACTIVATION SHOW THAT IT IS A NOVEL TYPE OF SERINE-PROTEASE

1987 ◽  
Author(s):  
F Tokunaga ◽  
T Miyata ◽  
T Nakamura ◽  
T Morita ◽  
S Iwanaga
Keyword(s):  
Serine Protease ◽  
Heavy Chain ◽  
Light Chain ◽  
Interleukin 2 ◽  
Coagulation Factor ◽  
Clotting Factor ◽  
Single Chain ◽  
Terminal Sequence ◽  
A Chain ◽  
Factor C

Limulus clotting factor, factor C, is a lipopolysaccharide (LPS)-sensitive serine-protease zymogen present in the hemocytes. It is a two-chain glycoprotein (M.W. = 123,000) composed of a heavy chain (M.W. = 80,000) and a light chain (M.W. = 43,000) T. Nakamura et al. (1986) Eur. J. Biochem. 154, 511-521 .On further studies of this zymogen, a single-chain factor C (M.W. = 123,000) was identified by Western blotting technique. The heavy chain had an NH2-terminal sequence of Ser-Gly-Val-Asp-, which was consistent with the NH2-terminal sequence of the single-chain factor C, indicating that the heavy chain is located in the NH2-terminal part of the zymogen. The light chain had an NH22-terminal sequence of Ser-Ser-Gln-Pro-. Incubation of the two-chain zymogen with LPS resulted in the cleavage of a Phe-Ile bond between residues 72 and 73 of the light chain. Concomitant with this cleavage, the A (72.amino acids) and B chains derived from the light chain was formed. The complete amino acid sequence of the A chain was determined by automated Edman degradation. The A chain contained a typical segment which is similar structuraly to those a family of repeats in human β2 -glycoprotein I, complement factors B, Clr, Cls, H, C4b-binding protein, 02, coagulation factor XIII b subunit, haptoglobin a chain, and interleukin 2 receptor. The NH2-terminal sequence of the B chain was Ile-Trp-Asn-Gly-. This chain contained the serine-active site sequence of -ASP-Ala-Cys-Ser-Gly-Asp-SER-Gly-Gly-Pro-.These results indicate that limulus factor C exists in the hemocytes in a single-chain zymogen form and is converted to an active serine-protease by hydrolysis of a specific Phe-Ile peptide bond. The correlation of limulus factor C and mammalian complement proteins was also suggested.

A unique substituted Co(ii)-formate coordination framework exhibits weak ferromagnetic single-chain-magnet like behavior

2012 ◽  
Vol 48 (52) ◽  
pp. 6568 ◽  
Author(s):  
Jiong-Peng Zhao ◽  
Qian Yang ◽  
Zhong-Yi Liu ◽  
Ran Zhao ◽  
Bo-Wen Hu ◽  
...  
Keyword(s):  
Single Chain ◽  
Coordination Framework ◽  
Weak Ferromagnetic

Assembling Magnetic Nanowires into Networks: A Layered CoII Carboxylate Coordination Polymer Exhibiting Single-Chain-Magnet Behavior

2006 ◽  
Vol 118 (38) ◽  
pp. 6458-6462 ◽  
Author(s):  
Yan-Zhen Zheng ◽  
Ming-Liang Tong ◽  
Wei-Xiong Zhang ◽  
Xiao-Ming Chen
Keyword(s):  
Coordination Polymer ◽  
Magnetic Nanowires ◽  
Single Chain

scholarly journals The Structure of Amyloid Versus the Structure of Globular Proteins

2020 ◽  
Vol 21 (13) ◽  
pp. 4683 ◽  
Author(s):  
Piotr Fabian ◽  
Mateusz Banach ◽  
Katarzyna Stapor ◽  
Leszek Konieczny ◽  
Magdalena Ptak-Kaczor ◽  
...  
Keyword(s):  
Gaussian Distribution ◽  
Experimental Studies ◽  
Data Bank ◽  
Globular Proteins ◽  
Hydrophobic Core ◽  
Single Chain ◽  
Spherical Micelle ◽  
Globular Structure ◽  
A Chain ◽  
High Level

The issue of changing the structure of globular proteins into an amyloid form is in the focus of researchers' attention. Numerous experimental studies are carried out, and mathematical models to define the essence of amyloid transformation are sought. The present work focuses on the issue of the hydrophobic core structure in amyloids. The form of ordering the hydrophobic core in globular proteins is described by a 3D Gaussian distribution analog to the distribution of hydrophobicity in a spherical micelle. Amyloid fibril is a ribbon-like micelle made up of numerous individual chains, each representing a flat structure. The distribution of hydrophobicity within a single chain included in the fibril describes the 2D Gaussian distribution. Such a description expresses the location of polar residues on a circle with a center with a high level of hydrophobicity. The presence of this type of order in the amyloid forms available in Preotin Data Bank (PDB) (both in proto- and superfibrils) is demonstrated in the present work. In this system, it can be assumed that the amyloid transformation is a chain transition from 3D Gauss ordering to 2D Gauss ordering. This means changing the globular structure to a ribbon-like structure. This observation can provide a simple mathematical model for simulating the amyloid transformation of proteins.

A one dimensional coordination polymer composed of antiferromagnetically coupled disk-like [Mn7] units

CrystEngComm ◽  
2018 ◽  
Vol 20 (43) ◽  
pp. 6963-6969
Author(s):  
En-Che Yang ◽  
Han-Sheng Huang ◽  
Shao-Yun Huang ◽  
Shi-Yi Huang ◽  
Yu-Ying Chang ◽  
...  
Keyword(s):  
Coordination Polymer ◽  
Single Chain ◽  
One Dimensional

A single-chain magnet (SCM) was constructed from disk-like Mn7 clusters linked by azide units.

A Zinc(II) Coordination Polymer Based on a Chain of {Zn 2 O 7 } Bitetrahedra Bridged by 3‐Methoxybenzoates

2020 ◽  
Vol 5 (31) ◽  
pp. 9820-9824
Author(s):  
Pooja H. Bhargao ◽  
Venkatesha R. Hathwar ◽  
Bikshandarkoil R. Srinivasan
Keyword(s):  
Coordination Polymer ◽  
A Chain

Preparation and Structural Characterization of Chain Ni (II) Coordination Polymer Material

2011 ◽  
Vol 322 ◽  
pp. 369-372
Author(s):  
Zhi Xiang Ji
Keyword(s):  
Coordination Polymer ◽  
Polymer Material ◽  
Chain Structure ◽  
Monoclinic Space Group ◽  
Dimensional Chain ◽  
X Ray Diffraction ◽  
One Dimensional ◽  
X Ray ◽  
A Chain

A chain Ni (II) coordination polymer material was prepared and characterized by elemental analysis and single-crystal X-ray diffraction. It crystallizes in monoclinic, space group C2/c with a = 1.24348(13) nm, b = 1.29477(12) nm, c = 1.51480(17) nm and Dc = 1.401 g•cm-3. The results of structural analysis indicated that each Ni (II) ion forms six-coordinated with nitrogen atoms of pyridine and thiocyanate, and the Ni (II) coordination polymer material formed one dimensional chain structure by the interaction of pyridine rings.

A robust two-dimensional zirconium-based luminescent coordination polymer built on a V-shaped dicarboxylate ligand for vapor phase sensing of volatile organic compounds

2018 ◽  
Vol 54 (58) ◽  
pp. 8088-8091 ◽  
Author(s):  
Pei-Yao Du ◽  
William P. Lustig ◽  
Simon J. Teat ◽  
Wen Gu ◽  
Xin Liu ◽  
...  
Keyword(s):  
Volatile Organic Compounds ◽  
Coordination Polymer ◽  
Organic Compounds ◽  
Vapor Phase ◽  
Two Dimensional ◽  
Volatile Organic ◽  
Dicarboxylate Ligand

We report herein a new two-dimensional zirconium-based luminescent coordination polymer exhibiting selective fluorescence responses towards a variety of volatile organic compounds upon exposure in the vapor phase.

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