Adsorption of Benzene on Cu(100) and on Cu(100) Covered with an Ultrathin NaCl Film: Molecule–Substrate Interaction and Decoupling

2015 ◽  
Vol 119 (8) ◽  
pp. 4062-4071 ◽  
Author(s):  
Maitreyi Robledo ◽  
Gianfranco Pacchioni ◽  
Fernando Martín ◽  
Manuel Alcamí ◽  
Sergio Díaz-Tendero
Keyword(s):  
Substrate Interaction

Effects of Ni catalyst–substrate interaction on carbon nanotubes growth by CVD

2007 ◽  
Vol 37 (1-2) ◽  
pp. 21-25 ◽  
Author(s):  
G.P. Veronese ◽  
R. Rizzoli ◽  
R. Angelucci ◽  
M. Cuffiani ◽  
L. Malferrari ◽  
...  
Keyword(s):  
Carbon Nanotubes ◽  
Ni Catalyst ◽  
Substrate Interaction

scholarly journals Unbinding of Hyaluronan Accelerates the Enzymatic Activity of Bee Hyaluronidase

2011 ◽  
Vol 286 (41) ◽  
pp. 35699-35707 ◽  
Author(s):  
Attila Iliás ◽  
Károly Liliom ◽  
Brigitte Greiderer-Kleinlercher ◽  
Stephan Reitinger ◽  
Günter Lepperdinger
Keyword(s):  
Experimental Data ◽  
Quartz Crystal ◽  
Surface Loop ◽  
X Ray ◽  
Site Model ◽  
Substrate Interaction ◽  
Close Proximity ◽  
Binding Groove ◽  
The One ◽  
Best Fit

Hyaluronan (HA), a polymeric glycosaminoglycan ubiquitously present in higher animals, is hydrolyzed by hyaluronidases (HAases). Here, we used bee HAase as a model enzyme to study the HA-HAase interaction. Located in close proximity to the active center, a bulky surface loop, which appears to obstruct one end of the substrate binding groove, was found to be functionally involved in HA turnover. To better understand kinetic changes in substrate interaction, binding of high molecular weight HA to catalytically inactive HAase was monitored by means of quartz crystal microbalance technology. Replacement of the delimiting loop by a tetrapeptide interconnection increased the affinity for HA up to 100-fold, with a KD below 1 nm being the highest affinity among HA-binding proteins surveyed so far. The experimental data of HA-HAase interaction were further validated showing best fit to the theoretically proposed sequential two-site model. Besides the one, which had been shown previously in course of x-ray structure determination, a previously unrecognized binding site works in conjunction with an unbinding loop that facilitates liberation of hydrolyzed HA.

scholarly journals Potent Anticoagulant Aptamer Directed against Factor IXa Blocks Macromolecular Substrate Interaction

2012 ◽  
Vol 287 (16) ◽  
pp. 12779-12786 ◽  
Author(s):  
Bruce Sullenger ◽  
Rebecca Woodruff ◽  
Dougald M. Monroe
Keyword(s):  
Substrate Interaction ◽  
Factor Ixa
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