Comparative study of hydration shell dynamics around a hyperactive antifreeze protein and around ubiquitin

2014 ◽  
Vol 141 (22) ◽  
pp. 22D529 ◽  
Author(s):  
Elise Duboué-Dijon ◽  
Damien Laage
Keyword(s):  
Comparative Study ◽  
Hydration Shell ◽  
Antifreeze Protein ◽  
Hydration Shell Dynamics ◽  
Shell Dynamics

Slow-to-fast transition of hydrogen bond dynamics in acetamide hydration shell formation

2015 ◽  
Vol 17 (16) ◽  
pp. 10987-10992 ◽  
Author(s):  
Francesco D'Amico ◽  
Barbara Rossi ◽  
Gaia Camisasca ◽  
Filippo Bencivenga ◽  
Alessandro Gessini ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Hydration Shell ◽  
Shell Formation ◽  
Hydrogen Bond Dynamics ◽  
Hydration Shell Dynamics ◽  
Water Amount ◽  
Shell Dynamics

The acetamide hydration shell dynamics speeds up in a remarkable way upon increasing the water amount.

scholarly journals Calcium-Binding Generates the Semi-Clathrate Waters on a Type II Antifreeze Protein to Adsorb onto an Ice Crystal Surface

Biomolecules ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 162 ◽  
Author(s):  
Tatsuya Arai ◽  
Yoshiyuki Nishimiya ◽  
Yasushi Ohyama ◽  
Hidemasa Kondo ◽  
Sakae Tsuda
Keyword(s):  
Binding Site ◽  
Calcium Binding ◽  
Crystal Surface ◽  
Hydration Shell ◽  
Antifreeze Protein ◽  
Bound State ◽  
Ice Crystal ◽  
Prism Plane ◽  
Ice Binding ◽  
Significant Difference

Hydration is crucial for a function and a ligand recognition of a protein. The hydration shell constructed on an antifreeze protein (AFP) contains many organized waters, through which AFP is thought to bind to specific ice crystal planes. For a Ca2+-dependent species of AFP, however, it has not been clarified how 1 mol of Ca2+-binding is related with the hydration and the ice-binding ability. Here we determined the X-ray crystal structure of a Ca2+-dependent AFP (jsAFP) from Japanese smelt, Hypomesus nipponensis, in both Ca2+-bound and -free states. Their overall structures were closely similar (Root mean square deviation (RMSD) of Cα = 0.31 Å), while they exhibited a significant difference around their Ca2+-binding site. Firstly, the side-chains of four of the five Ca2+-binding residues (Q92, D94 E99, D113, and D114) were oriented to be suitable for ice binding only in the Ca2+-bound state. Second, a Ca2+-binding loop consisting of a segment D94–E99 becomes less flexible by the Ca2+-binding. Third, the Ca2+-binding induces a generation of ice-like clathrate waters around the Ca2+-binding site, which show a perfect position-match to the waters constructing the first prism plane of a single ice crystal. These results suggest that generation of ice-like clathrate waters induced by Ca2+-binding enables the ice-binding of this protein.

Unusual structural properties of water within the hydration shell of hyperactive antifreeze protein

2014 ◽  
Vol 141 (5) ◽  
pp. 055103 ◽  
Author(s):  
Anna Kuffel ◽  
Dariusz Czapiewski ◽  
Jan Zielkiewicz
Keyword(s):  
Structural Properties ◽  
Hydration Shell ◽  
Antifreeze Protein

Author response for "Laminar distribution of cortical projection neurons to the pulvinar: A comparative study in cats and mice"

2020 ◽  
Author(s):  
Bruno Oliveira Ferreira de Souza ◽  
Éve‐Marie Frigon ◽  
Robert Tremblay‐Laliberté ◽  
Christian Casanova ◽  
Denis Boire
Keyword(s):  
Comparative Study ◽  
Author Response ◽  
Projection Neurons ◽  
Cortical Projection ◽  
Laminar Distribution

Structural and functional properties of Escherichia coli-derived nucleoplasmin A comparative study of recombinant and natural proteins

2001 ◽  
Vol 268 (6) ◽  
pp. 1739-1748
Author(s):  
Aitor Hierro ◽  
Jesus M. Arizmendi ◽  
Javier De Las Rivas ◽  
M. Angeles Urbaneja ◽  
Adelina Prado ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Comparative Study ◽  
Functional Properties ◽  
Structural And Functional Properties
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