2012_02_11 Dear All, Two really striking examples of "Intrinsically Flexible Proteins" are:
(1) Adenylate kinase: Vonrhein, Schlauderer & Schulz (1995) Structure 3, 483 “Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases” http://portal.uni-freiburg.de/structbio/structuregallery/ak_folder/mpeg in particular look at: "video as MPEG white background, closing & opening enzyme (707kb)" Each "black dot" [upper left, in the morph] indicates an observed crystal structure. (2) Lac repressor: see Proteopedia page on lac repressor, morphing from the structure bound to its cognate DNA, to that of the structure bound to its the non-cognate DNA, at: http://proteopedia.org/w/Lac_repressor best regards, Joel On 10 Feb 2012, at 22:51, Jacob Keller wrote: Interesting to juxtapose these two responses: James Stroud: How could they not be snapshots of conformations adopted in solution? David Schuller: How could that possibly be the case when any structure is an average of all the unit cells of the crystal over the timespan of the diffraction experiment? JPK ******************************************* Jacob Pearson Keller Northwestern University Medical Scientist Training Program email: j-kell...@northwestern.edu<mailto:j-kell...@northwestern.edu> *******************************************
