Intrinsically Disordered Protein: Difference between revisions

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Eric Martz (talk | contribs)
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== Many IUPs undergo disorder-order transition ==
== Many IUPs undergo disorder-order transition ==


Binding of natural ligands such as a variety of small molecules, substrates, cofactors, other proteins, nucleic acids or membranes induces folding of unstructured proteins. See the following two examples and also the page on [http://www.proteopedia.org/wiki/index.php/Lac_repressor Lac repressor]
Binding of natural ligands such as a variety of small molecules, substrates, cofactors, other proteins, nucleic acids or membranes may induce folding of unstructured proteins. In addition to the cases detailed below, other examples include [[1g3j]], [[1oct]]<ref name="tompa2002" />, and the  [http://www.proteopedia.org/wiki/index.php/Lac_repressor Lac repressor].


=== The human p27<sup>Kip1</sup> kinase inhibitory domain <ref>PMID: 8684460</ref> ===
=== The human p27<sup>Kip1</sup> kinase inhibitory domain <ref>PMID: 8684460</ref> ===

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Tzviya Zeev-Ben-Mordehai, Eric Martz, Jaime Prilusky, Eran Hodis, Wayne Decatur, Joel L. Sussman, Karl Oberholser, David Canner, Alexander Berchansky, Michal Harel