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One of the aspartates that formerly interacted with the tyrosine now forms a hydrogen bond with a conserved histidine.
None of the sulfide ions make any favorable hydrogen bond to the protein.
Its frequency depends on the strength of the hydrogen bond.
The reason for this is easily understood since ammonia forms a hydrogen bond that imidazole (or histidine) cannot form.
Furthermore, simulated annealing does not provide well-defined conformations, but the different conformations that are observed are consistent with several possible hydrogen bond combinations.
The transition is opposed by the loss in conformational entropy, and driven by gains in free energy due to hydrophobic burial and hydrogen bond formation.
The environment of the iron-sulfur cluster is not exceptional having, on average, one hydrogen bond per liganding cysteine and otherwise a surrounding hydrophobic environment.
Note the hydrogen bond between the exocyclic amine of the 3h cytosine base and the non-bridging oxygen of the phosphate at the exchange point.
Unlike the alcohols, general anaesthetics cannot hydrogen bond to phospholipid headgroups.
The second condition ensures that the hydrogen bond is more or less linear.
The second distance restraint restricts the angle of the hydrogen bond.
To represent the key feature of a polar solvent like water, the capability of hydrogen bond formation has to be represented.
Formally, the hydrogen bond has to be treated as a combination of a dipole-dipole interaction and a charge transfer reaction.
The relation should be particularly useful in studies of enzyme catalytic sites or other protein-ligand interactions in which hydrogen bond strength may play a key role.
Correlation with hydrogen bond length.
