Molecular recognition: hydrogen-bonding receptors that function in highly competitive solvents

1993 ◽  
Vol 115 (1) ◽  
pp. 369-370 ◽  
Author(s):  
Erkang Fan ◽  
Scott A. Van Arman ◽  
Scott Kincaid ◽  
Andrew D. Hamilton
2021 ◽  
Author(s):  
Hong Zhang ◽  
Li-Li Wang ◽  
Xin-Yu Pang ◽  
Liu-Pan Yang ◽  
Wei Jiang

A water-soluble tetralactam macrocycle with 2,6-diethoxynaphthalene group as side walls is able to strongly bind riboflavin (Ka >107 M−1) in water through hydrogen bonding and the hydrophobic effect. The encapsulated...


1995 ◽  
Vol 1995 (8) ◽  
pp. 1575-1578
Author(s):  
Burkhard König ◽  
Oliver Möller ◽  
Peter G. Jones ◽  
Birte Ahrens

2018 ◽  
Vol 74 (7) ◽  
pp. 690-694 ◽  
Author(s):  
Ian W. Windsor ◽  
Ronald T. Raines

Crystal structures of inactive variants of HIV-1 protease bound to peptides have revealed how the enzyme recognizes its endogenous substrates. The best of the known substrates is, however, a nonnatural substrate that was identified by directed evolution. The crystal structure of the complex between this substrate and the D25N variant of the protease is reported at a resolution of 1.1 Å. The structure has several unprecedented features, especially the formation of additional hydrogen bonds between the enzyme and the substrate. This work expands the understanding of molecular recognition by HIV-1 protease and informs the design of new substrates and inhibitors.


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