Practical Guide to Homology Modeling: Difference between revisions
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Although fold is required for the function of most proteins, some proteins are [[Intrinsically Disordered Protein|intrinsically disordered]] (natively unstructured) and do not fold, at least by themselves. Often, intrinsically disordered protein transitions to an ordered state when it binds to a folded partner protein. However some proteins remain disordered while performing their functions. | Although fold is required for the function of most proteins, some proteins are [[Intrinsically Disordered Protein|intrinsically disordered]] (natively unstructured) and do not fold, at least by themselves. Often, intrinsically disordered protein transitions to an ordered state when it binds to a folded partner protein. However some proteins remain disordered while performing their functions. | ||
By some estimates, 10% of proteins are intrinsically disordered for their full lengths, and about 40% of eukaryotic proteins have at least one loop 50 residues or longer that is intrinsically disordered. These disordered loops are typically missing from X-ray crystallographic structures because the disorder blurs that portion of the electron density map. | By some estimates, 10% of proteins are intrinsically disordered for their full lengths, and about 40% of eukaryotic proteins have at least one loop 50 residues or longer that is intrinsically disordered<ref>PMID:12368089</ref>. These disordered loops are typically missing from X-ray crystallographic structures because the disorder blurs that portion of the electron density map. | ||
Examples: | Examples: | ||
