Structural Dynamics of Dimethyl Sulfoxide Aqueous Solutions Investigated by Ultrafast Infrared Spectroscopy: Using Thiocyanate Anion as a Local Vibrational Probe

2018 ◽  
Vol 122 (50) ◽  
pp. 12131-12138 ◽  
Author(s):  
Qianshun Wei ◽  
Dexia Zhou ◽  
Xiaoqian Li ◽  
Yuwan Chen ◽  
Hongtao Bian
Keyword(s):  
Infrared Spectroscopy ◽  
Aqueous Solutions ◽  
Dimethyl Sulfoxide ◽  
Structural Dynamics ◽  
Thiocyanate Anion ◽  
Ultrafast Infrared

New Possibilities of Investigating Nucleic Acids and Nucleoproteins in Aqueous Solutions by Infrared Spectroscopy

Nature ◽  
1972 ◽  
Vol 235 (5338) ◽  
pp. 386-388 ◽  
Author(s):  
M. SHIE ◽  
I. G. KHARITONENKOV ◽  
T. I. TIKHONENKO ◽  
Yu. N. CHIRGADZE
Keyword(s):  
Infrared Spectroscopy ◽  
Nucleic Acids ◽  
Aqueous Solutions

scholarly journals Structural dynamics of the Ca2+-ATPase studied by time-resolved infrared spectroscopy

2008 ◽  
Vol 22 (2-3) ◽  
pp. 63-82 ◽  
Author(s):  
Andreas Barth
Keyword(s):  
Infrared Spectroscopy ◽  
Structural Dynamics ◽  
Ground State ◽  
Transfer Reaction ◽  
High Reactivity ◽  
Acetyl Phosphate ◽  
Time Resolved ◽  
Closed Conformation ◽  
Sarcoplasmic Reticulum Membrane ◽  
Time Resolved Infrared Spectroscopy

This review discusses the contribution of time-resolved infrared spectroscopy to the understanding of the Ca2+pump in the sarcoplasmic reticulum membrane of skeletal muscle cells (SERCA1a). The focus is on interactions of the substrate ATP with the ATPase and on the bond parameters of the phosphoenzyme phosphate group. Functional groups throughout the ATP molecule are important for stabilising the closed conformation of the ATP–ATPase complex and for fast phosphorylation of the ATPase. Dissociation of the reaction product ADP after phosphorylation leads to a more open average conformation of the enzyme and does not trigger the transition from the first phosphoenzyme Ca2E1P to the second E2P. The P–O bond between phosphate and aspartyl moieties is weaker in Ca2E1P and E2P than in acetyl phosphate in aqueous solution, which explains the high reactivity of the phosphoenzymes. This ground state property of the phosphoenzymes prepares for a phosphate transfer reaction with dissociative character.

Ultrafast Infrared Spectroscopy of Protein Dynamics

1993 ◽  
pp. 517-521 ◽  
Author(s):  
R. M. Hochstrasser ◽  
R. Diller ◽  
S. Maiti ◽  
T. Lian ◽  
B. Locke ◽  
...  
Keyword(s):  
Infrared Spectroscopy ◽  
Protein Dynamics ◽  
Ultrafast Infrared
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