Note that the appearance of a binding site in this MWC context serves only to indicate the increased probability of a binding-competent conformer; though not initially shown in the model, those binding-competent conformers would always be present in the ensemble).
Other causes of misfolding and misfunction include point mutation(s), exposure to internal or external toxins, impaired posttranslational modifications (phosphorylation, advanced glycation, deamidation, racemization, acetylation, etc)., an increased probability of degradation, impaired trafficking, loss of binding partners or oxidative damage.
Given that one glycosylation site can carry oligosaccharides with many different structures, the net effect would likely be an increased probability of any given secretor glycopeptide binding to AAL.
Often, misfolding and misfunction originate from point mutation(s) or result from an exposure to internal or external toxins, impaired posttranslational modifications (phosphorylation, advanced glycation, deamidation, racemization, etc)., an increased probability of degradation, impaired trafficking, lost binding partners or oxidative damage.
Misfolding and misfunction can originate from point mutation(s) or result from an exposure to internal or external toxins, from impaired posttranslational modification (phosphorylation, advanced glycation, deamidation, racemization, etc)., from an increased probability of degradation, from impaired trafficking, from lost binding partners or from oxidative damage among other causes.
Increased probability of prompt citations.
