Examples of allosteric

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Energetic components of the allosteric machinery in hemoglobin measured by hydrogen exchange.
The term ' allosteric ' means that these proteins mediate indirect interactions between sites that are physically separated on the protein.
Structural kinetics of the allosteric transition of aspartate transcarbamylase produced by physiological substrates.
Mutations affecting the glycine receptor agonist transduction mechanism convert the competitive antagonist, picrotoxin, into an allosteric potentiator.
The intramolecular interactions that govern the behaviour of allosteric enzymes are indeed many and complex.
In recent years, molecular cloning and site-directed mutagenesis of ion channels have enabled new insights into the structural basis of the allosteric transitions.
Moreover, proteins that undergo allosteric rearrangements and have multiple stable conformations separated by small energy differences can be affected by lattice forces.
Developing allosteric inhibitors to these enzymes may yield ways to prevent non-specific binding to the active sites of off-target proteases.
An allosteric enzyme model with positive feedback applied to glycolytic oscillations.
This demonstrated a general principle, since many enzymes and other proteins exploit a similar ' allosteric ' structural change to switch a process on or off.
Unlike the quaternary structure transition, the tertiary structure change of the 240s loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion.
Localization of regions affecting an allosteric transition in cyclic nucleotide-activated channels.
Results of two extensive studies - on ribosomes and on the allosteric protein aspartate transcarbamoylase - illustrate the application of the various methods.
Structural differences between solution and crystal conformations are likely to be observed with increasing frequency in the case of allosteric enzymes, complexes or larger assemblies.
This novel allosteric mechanism has not previously been observed for nucleic acid catalysts.
Heterotypic channels are useful for investigation of interhemichannel allosteric and cooperative effects.
In these multisubunit proteins there may still be allosteric interactions within subunits ; but additionally, interactions between subunits strongly influence the conformational changes that govern function as measured experimentally.
When the allosteric regulation is weak, only a random enzymic activity has been found where the phases of each catalytic cycle of the individual enzyme are uniformly distributed.
These changes could be effected by allosteric effects on other transmembrane domains or by affecting entry into the pore, but are unlikely to line the pore in the usual sense.

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