reversible dimerization
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2021 ◽  
Author(s):  
Zhanyao Hou ◽  
Werner M. Nau ◽  
Richard Hoogenboom

The formation of supramolecular hydrogels is demonstrated based on ternary complexes between anthracene side-chain functionalized polymers and macrocyclic hosts. Photo-induced reversible dimerization enables switching between supramolecular and covalent hydrogels.


Molecules ◽  
2020 ◽  
Vol 26 (1) ◽  
pp. 108
Author(s):  
Alexey Chubarov ◽  
Anna Spitsyna ◽  
Olesya Krumkacheva ◽  
Dmitry Mitin ◽  
Daniil Suvorov ◽  
...  

Pulsed Dipolar Spectroscopy (PDS) methods of Electron Paramagnetic Resonance (EPR) were used to detect and characterize reversible non-covalent dimers of Human Serum Albumin (HSA), the most abundant protein in human plasma. The spin labels, MTSL and OX063, were attached to Cys-34 and these chemical modifications of Cys-34 did affect the dimerization of HSA, indicating that other post-translational modifications can modulate dimer formation. At physiologically relevant concentrations, HSA does form weak, non-covalent dimers with a well-defined structure. Dimer formation is readily reversible into monomers. Dimerization is very relevant to the role of HSA in the transport, binding, and other physiological processes.


2020 ◽  
Vol 358 ◽  
pp. 136903
Author(s):  
Andrey S. Mendkovich ◽  
Arona Ngom ◽  
Vladimir A. Kokorekin ◽  
Mikhail N. Mikhailov ◽  
Diariatou Gningue-Sall ◽  
...  

Mitochondrion ◽  
2019 ◽  
Vol 49 ◽  
pp. 149-155 ◽  
Author(s):  
Rabia Ramzan ◽  
Annika Rhiel ◽  
Petra Weber ◽  
Bernhard Kadenbach ◽  
Sebastian Vogt

Tetrahedron ◽  
2019 ◽  
Vol 75 (7) ◽  
pp. 912-920 ◽  
Author(s):  
Jonas Van Damme ◽  
Otto van den Berg ◽  
Joost Brancart ◽  
Guy Van Assche ◽  
Filip Du Prez

2017 ◽  
Vol 114 (47) ◽  
pp. 12572-12577 ◽  
Author(s):  
Allister Crow ◽  
Nicholas P. Greene ◽  
Elise Kaplan ◽  
Vassilis Koronakis

MacB is an ABC transporter that collaborates with the MacA adaptor protein and TolC exit duct to drive efflux of antibiotics and enterotoxin STII out of the bacterial cell. Here we present the structure of ATP-bound MacB and reveal precise molecular details of its mechanism. The MacB transmembrane domain lacks a central cavity through which substrates could be passed, but instead conveys conformational changes from one side of the membrane to the other, a process we term mechanotransmission. Comparison of ATP-bound and nucleotide-free states reveals how reversible dimerization of the nucleotide binding domains drives opening and closing of the MacB periplasmic domains via concerted movements of the second transmembrane segment and major coupling helix. We propose that the assembled tripartite pump acts as a molecular bellows to propel substrates through the TolC exit duct, driven by MacB mechanotransmission. Homologs of MacB that do not form tripartite pumps, but share structural features underpinning mechanotransmission, include the LolCDE lipoprotein trafficking complex and FtsEX cell division signaling protein. The MacB architecture serves as the blueprint for understanding the structure and mechanism of an entire ABC transporter superfamily and the many diverse functions it supports.


2017 ◽  
Vol 18 (10) ◽  
pp. 3457-3468 ◽  
Author(s):  
Ido Rosenbaum ◽  
Ram Avinery ◽  
Assaf J. Harnoy ◽  
Gadi Slor ◽  
Einat Tirosh ◽  
...  

2017 ◽  
Vol 53 (65) ◽  
pp. 9059-9062 ◽  
Author(s):  
Jochen R. Brandt ◽  
Lubomír Pospíšil ◽  
Lucie Bednárová ◽  
Rosenildo Correa da Costa ◽  
Andrew J. P. White ◽  
...  

Electrochemically-reversible dimerisation of an azoniahelicene provides a chiroptical switching system that exhibits significant hysteresis and thereby a large area of bistability.


2017 ◽  
Vol 8 (48) ◽  
pp. 7515-7528 ◽  
Author(s):  
Julian P. Chesterman ◽  
Fei Chen ◽  
Amanda J. Brissenden ◽  
Brian G. Amsden

With the objective of generating photo-responsive polymers, carbonate monomers with pendant cinnamoyl or coumarin moieties, which are capable of photo-reversible dimerization, were synthesized.


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