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This result demonstrates how complex and unexpected higher orders of binding regulation can be.
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For example, activities of HS samples such as protein binding, enzyme inhibition, and cell regulation can be measured and related to domain structure.
Different steps in the complex dynamic regulation can be characterized by ligand binding kinetics.
Such regulation can be achieved by autophosphorylation or interactions with other domains or binding partners.
Such regulation can be mediated by cis-acting sequence elements that interact with RNA-binding proteins.
Gene translation regulation can be affected by multiple factors such as 5′- or 3′- untranslated regions (UTRs) composition, mRNA structure, RNA binding protein (RBP), and ribosomal proteins.
It also argues legally binding self-regulation can be introduced far more quickly than any statutory solution and can, if devised correctly, be equally effective.
As a consequence, binding at a site of target up-regulation can be rapid, a property that would be valuable in the context of a clinical contrast agent.
Practical information that explains these regulations can be placed in non-binding attachments to a legal act [41].
Competitive or allosteric regulation by ligand binding can be cooperative if the enzymes form oligomers, as in the case of hemoglobin (Perutz, 1989).
The coupled CRIB and PDZ architecture of Par-6 reveals how simple binding domains can be combined to yield complex regulation.
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