Search results
Results from the WOW.Com Content Network
The thiourea hydrogen bonds to the nitro group and stabilizes the incoming negative charge, while the amine acts a specific base to activate the nucleophile. This is an example of bifunctional catalysis. Hydrogen-bond catalysis is a type of organocatalysis that relies on use of hydrogen bonding interactions to accelerate and control organic ...
Hydrogen bond: A hydrogen bond is a specific type of dipole-dipole interaction between a partially positive hydrogen atom and a partially negative electron donor that contain a pair of electrons such as oxygen, fluorine and nitrogen. The strength of hydrogen bond depends on the chemical nature and geometric arrangement of each group.
Researchers have since conducted increasingly detailed investigations of the triad's exact catalytic mechanism. Of particular contention in the 1990s and 2000s was whether low-barrier hydrogen bonding contributed to catalysis, [18] [19] [20] or whether ordinary hydrogen bonding is sufficient to explain the mechanism.
The active site cavity consists of a network of side chains of several residues associated by hydrogen bonding, extending from the aqueous ligand of the metal. Of note, the highly conserved residue Tyr34 plays a key role in the hydrogen-bonding network, as nitration of this residue inhibits the protein's catalytic ability. [ 8 ]
Hydrogen-bonding between thiourea derivatives and carbonyl substrates involve two hydrogen bonds provided by coplanar amino substituents in the (thio)urea. [2] [3] [4][5] Squaramide catalysts engage in double H-bonding interactions and are often superior to thioureas.
The ribose zipper is an RNA tertiary structural element in which two RNA chains are held together by hydrogen bonding interactions involving the 2’OH of ribose sugars on different strands. The 2'OH can behave as both hydrogen bond donor and acceptor, which allows formation of bifurcated hydrogen bonds with another 2’ OH. [46] [47]
A study using human cells found that the nucleotide excision repair (NER) nucleases ERCC1-XPF and ERCC1-XPG induced genetic instability. [38] These enzymes cleave H-DNA at the loop formed by the two Hoogsteen hydrogen-bonded strands and the 5' end of the other Watson-Crick hydrogen-bonded strand, respectively. [38]
The active site for pyruvate dehydrogenase (image created from ) holds TPP through metal ligation to a magnesium ion (purple sphere) and through hydrogen bonding to amino acids. While over 20 amino acids can be found in the active site, amino acids Tyr 89, Arg 90, Gly 136, Val 138, Asp 167, Gly 168, Ala 169, Asn, 196, and His 263 actually ...