Intrinsically unfolded proteins (IUP) are a family of proteins characterized by the lack of stable folding. It means that they are very flexible and adopt many different conformations. Among the specific properties of IUPs their plasticity and promiscuity for interaction partners are very relevant. The intrinsic flexibility of IUPs allow them to adapt themselves to the shape of many partners, in a process that it is globally known as "induced folding". Here you have a good example of the induced folding of the protein TPP1 (white ribbon), interacting with the POT1 protein (orange surface) forming a complex involved in telomere maintenance. The induced folding of TPP1 helped by POT1 is very dynamic and economic if we consider the number of aminoacids involved (PDB code: 7S1T)
#molecularart ... #immolecular ... #IUP ... #intrinsicallyunfolded ... #flexibility ... #dynamic ... #interaction ... #promiscuity ... #POT1 ... #TPP1 ... #complex ... #telomere ... #inducedfolding ... #xray
POT1-TPP1 complex rendered with @proteinimaging and represented with @corelphotopaint
#molecularart ... #immolecular ... #IUP ... #intrinsicallyunfolded ... #flexibility ... #dynamic ... #interaction ... #promiscuity ... #POT1 ... #TPP1 ... #complex ... #telomere ... #inducedfolding ... #xray
POT1-TPP1 complex rendered with @proteinimaging and represented with @corelphotopaint
