crystallization nucleus
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Lubricants ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 1
Author(s):  
Andreas Conrad ◽  
Annika Hodapp ◽  
Bernhard Hochstein ◽  
Norbert Willenbacher ◽  
Karl-Heinz Jacob

This study investigates crystallization, melting and glass transition of Li- and Ca-12-hydroxystearate greases in relation to the pour point of the corresponding oils. The base oils for the greases are mineral oil, polyalphaolefin, alkylated naphthalene, propylene glycol, and trimellitate. For the mineral oil-based greases the crystallization temperature Tc increases and the melting temperature Tm decreases upon addition of thickener. The pour point of the mineral oil then is 3 K below Tc and does not properly define the lowest application temperature for mineral oil (MO) based greases. Both thickeners induce a small increase of the glass transition temperature (1–3 K) of the synthetic oils polyalphaolefin, alkylated naphthalene, propylene glycol. The pour point of the base oils correlates well with the onset of the glass transition in the corresponding grease indicated by a sharp increase in grease viscosity. Pure trimellitate with unbranched alkyl chains does not crystallize upon cooling but shows noticeable supercooling and cold crystallization. As the percentage of thickener in corresponding greases increases, more oil crystallizes upon cooling 20 K above the crystallization temperature of the trimellitate without thickener (−44 °C). Here, the thickener changes the crystallization behavior from homogeneous to heterogeneous and thus acts as a crystallization nucleus. The pour point of the base oil does not provide information on the temperature below which the greases stiffen significantly due to crystallization.


2015 ◽  
Vol 71 (10) ◽  
pp. 1235-1241 ◽  
Author(s):  
Anders Wiuf ◽  
Line Hyltoft Kristensen ◽  
Ole Kristensen ◽  
Jerzy Dorosz ◽  
Jonas Jensen ◽  
...  

The histone demethylase KDM5B is considered to be a promising target for anticancer therapy. Single-chain antibodies from llama (nanobodies) have been raised to aid in crystallization and structure determination of this enzyme. The antigen-binding properties of 15 of these nanobodies have been characterized. The crystal structure of one of these (NB17) has been determined to a resolution of 1.85 Å. NB17 crystallizes in space groupP4322 with six molecules in the asymmetric unit. The six molecules in the asymmetric unit pack as an entity with approximateD3 symmetry with interactions mediated by the CDR loops, which could act as a crystallization nucleus. NB17 does not bind to monomeric KDM5B residues 1–820, but is found to bind to aggregates formed after incubation at 310 K.


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