The covalently bound diazo group as an infrared probe for hydrogen bonding environments

2017 ◽  
Vol 19 (29) ◽  
pp. 19420-19426 ◽  
Author(s):  
Min You ◽  
Liyuan Liu ◽  
Wenkai Zhang
Keyword(s):  
Hydrogen Bonding ◽  
Diazo Group ◽  
Covalently Bound

The bandwidth or position of diazo groups can probe the polarizability and HBA, or density of HBD groups.

Covalently Bound Azido Groups Are Very Specific Water Sensors, Even in Hydrogen-Bonding Environments

2012 ◽  
Vol 116 (3) ◽  
pp. 1172-1179 ◽  
Author(s):  
Marta P. Wolfshorndl ◽  
Rachel Baskin ◽  
Ishita Dhawan ◽  
Casey H. Londergan
Keyword(s):  
Hydrogen Bonding ◽  
Covalently Bound

Hydrogen bonding in liquid methanol at ambient conditions and at high pressure

2000 ◽  
Vol 98 (3) ◽  
pp. 125-134 ◽  
Author(s):  
T. Weitkamp, J. Neuefeind, H. E. Fisch
Keyword(s):  
High Pressure ◽  
Hydrogen Bonding ◽  
Ambient Conditions

Fluorescence and pi-hydrogen bonding in naphthols

1968 ◽  
Vol 65 ◽  
pp. 1587-1589 ◽  
Author(s):  
Bithika Ghosh ◽  
Sadhan Basu
Keyword(s):  
Hydrogen Bonding

Adsorption of Fibrinogen and Fragment D of Fibrinogen onto the Insolubilized αChain of Fibrin

1979 ◽  
Vol 41 (04) ◽  
pp. 687-690
Author(s):  
F R Matthias
Keyword(s):  
Disulfide Bridges ◽  
Soluble Fibrin ◽  
Immobilized Proteins ◽  
Covalently Bound

SummaryAfter thrombin treatment insolubilized fibrinmonomer, which is obtained from insolubilized fibrinogen covalently bound to agarose, adsorbs soluble fibrin and its derivatives from solutions. The immobilized proteins are attached to the agarose by the ‘A’ αchain. After reduction of the disulfide bridges the β and γchains can be removed from the agarose.After thrombin treatment the immobilized αchain adsorbs fibrinogen and fragment D. To some extent the β and γchain do not seem necessary for the adsorption. The amount adsorbed increases, when thrombin treatment of the insolubilized protein follows the reduction process.This may indicate that the fibrinopeptides ‘A’ of the insolubilized αchain are better accessible after the removal of the β and γchains.

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