Probing conformational and functional substates of calmodulin by high pressure FTIR spectroscopy: influence of Ca2+ binding and the hypervariable region of K-Ras4B

2016 ◽  
Vol 18 (43) ◽  
pp. 30020-30028 ◽  
Author(s):  
Nelli Erwin ◽  
Satyajit Patra ◽  
Roland Winter
Keyword(s):  
High Pressure ◽  
Ftir Spectroscopy ◽  
Target Recognition ◽  
Hypervariable Region ◽  
Pressure Perturbation ◽  
Conformational Substates

Using pressure perturbation, conformational substates of CaM could be uncovered that conceivably facilitate target recognition by exposing the required binding surfaces.

Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa

2010 ◽  
Vol 66 (6) ◽  
pp. 654-663 ◽  
Author(s):  
Isabella Ascone ◽  
Carmelinda Savino ◽  
Richard Kahn ◽  
Roger Fourme
Keyword(s):  
High Pressure ◽  
Superoxide Dismutase ◽  
Bovine Erythrocyte ◽  
X Ray ◽  
X Ray Crystallography ◽  
Conformational Substates ◽  
Intermolecular Contacts ◽  
Uptake Process ◽  
Quaternary Structures ◽  
Electrostatic Loop

The 2 Å resolution crystal structure of bovine erythrocyte Cu,Zn superoxide dismutase (CuZnSOD) has been determined by X-ray diffraction at high pressure (0.57 GPa) and room temperature. At 0.57 GPa the secondary, tertiary and quaternary structures are similar to other previously determined bovine erythrocyte CuZnSOD structures. Nevertheless, pressure has a localized impact on the atomic coordinates of Cαatoms and on side chains. The compression of the crystal and of the protein backbone is anisotropic. This anisotropy is discussed, taking into account intermolecular contacts and protein conformation. Pressure perturbation highlights the more flexible zones in the protein such as the electrostatic loop. At 0.57 GPa, a global shift of the dimetallic sites in both subunits and changes in the oxidation state of Cu were observed. The flexibility of the electrostatic loop may be useful for the interaction of different metal carriers in the copper-uptake process, whereas the flexibility of the metal sites involved in the activity of the protein could contribute to explaining the ubiquitous character of CuZnSODs, which are found in organisms living in very different conditions, including the deep-sea environment. This work illustrates the potential of combining X-ray crystallography with high pressure to promote and stabilize higher energy conformational substates.

On the extraordinary pressure stability of the Thermotoga maritima arginine binding protein and its folded fragments – a high-pressure FTIR spectroscopy study

2020 ◽  
Vol 22 (20) ◽  
pp. 11244-11248 ◽  
Author(s):  
Michel W. Jaworek ◽  
Alessia Ruggiero ◽  
Giuseppe Graziano ◽  
Roland Winter ◽  
Luigi Vitagliano
Keyword(s):  
High Pressure ◽  
Ftir Spectroscopy ◽  
Thermotoga Maritima ◽  
Binding Protein ◽  
Spectroscopy Study ◽  
Pressure Stability ◽  
Truncated Variants

The domain swapped dimer of the arginine binding protein from Thermotoga maritima and its truncated variants are stable even at 10 kbar of pressure.

FTIR spectroscopy studies of high pressure-induced changes in pork macromolecular structure

2019 ◽  
Vol 1186 ◽  
pp. 377-383 ◽  
Author(s):  
S. Sazonova ◽  
M. Grube ◽  
K. Shvirksts ◽  
R. Galoburda ◽  
I. Gramatina
Keyword(s):  
High Pressure ◽  
Ftir Spectroscopy ◽  
Macromolecular Structure ◽  
Spectroscopy Studies ◽  
Induced Changes

A synthetic-dynamic method for water solubility measurements in high pressure CO 2 using ATR–FTIR spectroscopy

2016 ◽  
Vol 93 ◽  
pp. 386-391 ◽  
Author(s):  
Gurbuz Comak ◽  
Stéphanie Foltran ◽  
Jie Ke ◽  
Eduardo Pérez ◽  
Yolanda Sánchez-Vicente ◽  
...  
Keyword(s):  
High Pressure ◽  
Ftir Spectroscopy ◽  
Water Solubility ◽  
Dynamic Method
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