Coupling of global and local vibrational modes in dynamic allostery of proteins.
It is now recognized that internal global protein dynamics play an important role in the allosteric function of many proteins. Alterations of protein flexibility on effector binding affect the entropic cost of binding at a distant site. We present a coarse-grained model for a potential amplification of such entropic allostery due to coupling of fast, localized modes to the slow, global modes. We show how such coupling can give rise to large compensating entropic and enthalpic terms. The model corresponds to the pattern of calorimetry and NMR data from experiments on the Met repressor.
Hawkins
Rhoda J
RJ
Interdisciplinary Research Centre in Polymer Science and Technology, School of Physics and Astronomy and Astbury Centre for Structural Biology, University of Leeds, Leeds, United Kingdom.
McLeish
Tom C B
TC
D000494:Allosteric Regulation; D001059:Apoproteins / Q000737:chemistry; D002151:Calorimetry; D019277:Entropy; D029968:Escherichia coli Proteins / Q000737:chemistry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012097:Repressor Proteins / Q000737:chemistry; D014732:Vibration
D001059:Apoproteins; D029968:Escherichia coli Proteins; C053317:MetJ protein, E coli; D011506:Proteins; D012097:Repressor Proteins