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000023113 0247_ $$2DOI$$a10.1016/j.bpj.2011.12.031
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000023113 084__ $$2WoS$$aBiophysics
000023113 1001_ $$0P:(DE-Juel1)VDB78506$$aStadler, A.M.$$b0$$uFZJ
000023113 245__ $$aDynamics-Stability Relationships in Apo-and Holomyoglobin: A Combined Neutron Scattering and Molecular Dynamics Simulations Study
000023113 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2012
000023113 300__ $$a351 - 359
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000023113 440_0 $$0882$$aBiophysical Journal$$v102$$x0006-3495$$y2
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000023113 520__ $$aThe removal of the heme group from myoglobin (Mb) results in a destabilization of the protein structure. The dynamic basis of the destabilization was followed by comparative measurements on holo- (holo-Mb) and apomyoglobin (apo-Mb). Mean-squared displacements (MSD) and protein resilience on the picosecond-to-nanosecond timescale were measured by elastic incoherent neutron scattering. Differences in thermodynamic parameters, MSD, and resilience were observed for both proteins. The resilience of holo-Mb was significantly lower than that of apo-Mb, indicating entropic stabilization by a higher degree of conformational sampling in the heme-bound folded protein. Molecular dynamics simulations provided site-specific information. Averaged over the whole structure, the molecular dynamics simulations yielded similar MSD and resilience values for the two proteins. The mobility of residues around the heme group in holo-Mb showed a smaller MSD and higher resilience compared to the same residue group in apo-Mb. It is of interest that in holo-Mb, higher MSD values are observed for the residues outside the heme pocket, indicating an entropic contribution to protein stabilization by heme binding, which is in agreement with experimental results.
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000023113 650_2 $$2MeSH$$aAnimals
000023113 650_2 $$2MeSH$$aApoproteins: chemistry
000023113 650_2 $$2MeSH$$aEntropy
000023113 650_2 $$2MeSH$$aHeme: chemistry
000023113 650_2 $$2MeSH$$aHorses
000023113 650_2 $$2MeSH$$aMolecular Dynamics Simulation
000023113 650_2 $$2MeSH$$aMyoglobin: chemistry
000023113 650_2 $$2MeSH$$aNeutron Diffraction
000023113 650_2 $$2MeSH$$aProtein Stability
000023113 650_2 $$2MeSH$$aProtein Unfolding
000023113 650_2 $$2MeSH$$aTime Factors
000023113 650_2 $$2MeSH$$aTransition Temperature
000023113 650_7 $$00$$2NLM Chemicals$$aApoproteins
000023113 650_7 $$00$$2NLM Chemicals$$aMyoglobin
000023113 650_7 $$014875-96-8$$2NLM Chemicals$$aHeme
000023113 650_7 $$2WoSType$$aJ
000023113 7001_ $$0P:(DE-HGF)0$$aPellegrini, E.$$b1
000023113 7001_ $$0P:(DE-HGF)0$$aJohnson, M.$$b2
000023113 7001_ $$0P:(DE-HGF)0$$aFitter, J.$$b3
000023113 7001_ $$0P:(DE-HGF)0$$aZaccai, G.$$b4
000023113 773__ $$0PERI:(DE-600)1477214-0$$a10.1016/j.bpj.2011.12.031$$gVol. 102, p. 351 - 359$$n2$$p351 - 359$$q102<351 - 359$$tBiophysical journal$$v102$$x0006-3495$$y2012
000023113 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3260689
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