Heteroatom Tracing Reveals the 30-Atom Au–Ag Bimetallic Nanocluster as a Dimeric Structure

2020 ◽  
Vol 11 (17) ◽  
pp. 7307-7312
Author(s):  
Yingwei Li ◽  
Michael G. Taylor ◽  
Tian-Yi Luo ◽  
Yongbo Song ◽  
Nathaniel L. Rosi ◽  
...  
Keyword(s):  
Dimeric Structure

scholarly journals The dimeric structure of factor XI and zymogen activation

Blood ◽  
2013 ◽  
Vol 121 (19) ◽  
pp. 3962-3969 ◽  
Author(s):  
Yipeng Geng ◽  
Ingrid M. Verhamme ◽  
Stephen B. Smith ◽  
Mao-fu Sun ◽  
Anton Matafonov ◽  
...  
Keyword(s):  
Zymogen Activation ◽  
Factor Xi ◽  
Dimeric Structure ◽  
Key Points

Key Points FXI must be a dimer for normal activation by fXIIa but not for activation by thrombin or autoactivation. Poly-P is a cofactor for activation of coagulation fXI by fXIIa and thrombin and supports fXI autoactivation.

scholarly journals Structure and Stability of a Dimeric G-Quadruplex Formed by Cyclic Oligonucleotides

2010 ◽  
Vol 2010 ◽  
pp. 1-6 ◽  
Author(s):  
Joan Casals ◽  
Júlia Viladoms ◽  
Enrique Pedroso ◽  
Carlos González
Keyword(s):  
Telomeric Repeat ◽  
High Melting ◽  
Structure And Stability ◽  
Dimeric Structure ◽  
Nmr Data ◽  
High Melting Temperature ◽  
Sodium Nmr ◽  
G Quadruplex ◽  
Global Topology ◽  
Quadruplex Formation

We have studied the structure and stability of the cyclic dodecamer d<pGGGTTAGGGTTA>, containing two copies of the human telomeric repeat. In the presence of sodium, NMR data are consistent with a dimeric structure of the molecule in which two cycles self-associate forming a quadruplex with three guanine tetrads connected by edgewise loops. The two macrocycles are arranged in a parallel way, and the dimeric structure exhibits a high melting temperature. These results indicate that cyclization of the phosphodiester chain does not prevent quadruplex formation, although it affects the global topology of the quadruplex.

scholarly journals Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe–2S] cluster

2016 ◽  
Vol 72 (10) ◽  
pp. 732-737 ◽  
Author(s):  
Mohnad Abdalla ◽  
Ya-Nan Dai ◽  
Chang-Biao Chi ◽  
Wang Cheng ◽  
Dong-Dong Cao ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Sequence Alignment ◽  
Multiple Sequence Alignment ◽  
Active Site ◽  
Binding Pattern ◽  
Biological Functions ◽  
Structural Comparison ◽  
Multiple Sequence ◽  
Dimeric Structure

Glutaredoxins (Grxs) constitute a superfamily of proteins that perform diverse biological functions. TheSaccharomyces cerevisiaeglutaredoxin Grx6 not only serves as a glutathione (GSH)-dependent oxidoreductase and as a GSH transferase, but also as an essential [2Fe–2S]-binding protein. Here, the dimeric structure of the C-terminal domain of Grx6 (holo Grx6C), bridged by one [2Fe–2S] cluster coordinated by the active-site Cys136 and two external GSH molecules, is reported. Structural comparison combined with multiple-sequence alignment demonstrated that holo Grx6C is similar to the [2Fe–2S] cluster-incorporated dithiol Grxs, which share a highly conserved [2Fe–2S] cluster-binding pattern and dimeric conformation that is distinct from the previously identified [2Fe–2S] cluster-ligated monothiol Grxs.

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