Liquid phase behaviour in nonstoichiometric calcium-doped lanthanum chromites

1996 ◽  
Vol 31 (1) ◽  
pp. 157-163 ◽  
Author(s):  
J. D. Carter ◽  
M. M. Nasrallah ◽  
H. U. Anderson
ChemInform ◽  
2010 ◽  
Vol 24 (23) ◽  
pp. no-no
Author(s):  
N. SAKAI ◽  
T. KAWADA ◽  
H. YOKOKAWA ◽  
M. DOKIYA ◽  
I. KOJIMA

1993 ◽  
Vol 76 (3) ◽  
pp. 609-616 ◽  
Author(s):  
Natsuko Sakai ◽  
Tatsuya Kawada ◽  
Harumi Yokokawa ◽  
Masayuki Dokiya ◽  
Isao Kojima

Molecules ◽  
2020 ◽  
Vol 25 (20) ◽  
pp. 4705
Author(s):  
Adiran Garaizar ◽  
Ignacio Sanchez-Burgos ◽  
Rosana Collepardo-Guevara ◽  
Jorge R. Espinosa

Proteins containing intrinsically disordered regions (IDRs) are ubiquitous within biomolecular condensates, which are liquid-like compartments within cells formed through liquid–liquid phase separation (LLPS). The sequence of amino acids of a protein encodes its phase behaviour, not only by establishing the patterning and chemical nature (e.g., hydrophobic, polar, charged) of the various binding sites that facilitate multivalent interactions, but also by dictating the protein conformational dynamics. Besides behaving as random coils, IDRs can exhibit a wide-range of structural behaviours, including conformational switching, where they transition between alternate conformational ensembles. Using Molecular Dynamics simulations of a minimal coarse-grained model for IDRs, we show that the role of protein conformation has a non-trivial effect in the liquid–liquid phase behaviour of IDRs. When an IDR transitions to a conformational ensemble enriched in disordered extended states, LLPS is enhanced. In contrast, IDRs that switch to ensembles that preferentially sample more compact and structured states show inhibited LLPS. This occurs because extended and disordered protein conformations facilitate LLPS-stabilising multivalent protein–protein interactions by reducing steric hindrance; thereby, such conformations maximize the molecular connectivity of the condensed liquid network. Extended protein configurations promote phase separation regardless of whether LLPS is driven by homotypic and/or heterotypic protein–protein interactions. This study sheds light on the link between the dynamic conformational plasticity of IDRs and their liquid–liquid phase behaviour.


2002 ◽  
Vol 34 (6) ◽  
pp. 669-679 ◽  
Author(s):  
Claus Cagran ◽  
Christian Brunner ◽  
Achim Seifter ◽  
Gernot Pottlacher

2003 ◽  
Vol 206 (1-2) ◽  
pp. 61-85 ◽  
Author(s):  
A. Touriño ◽  
L.M. Casás ◽  
G. Marino ◽  
M. Iglesias ◽  
B. Orge ◽  
...  
Keyword(s):  

2007 ◽  
Vol 255 (2) ◽  
pp. 147-159 ◽  
Author(s):  
Blanca Estela García-Flores ◽  
Arturo Trejo ◽  
Jacinto Águila-Hernández

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