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>
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