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@ARTICLE{Stadler:23113,
      author       = {Stadler, A.M. and Pellegrini, E. and Johnson, M. and
                      Fitter, J. and Zaccai, G.},
      title        = {{D}ynamics-{S}tability {R}elationships in {A}po-and
                      {H}olomyoglobin: {A} {C}ombined {N}eutron {S}cattering and
                      {M}olecular {D}ynamics {S}imulations {S}tudy},
      journal      = {Biophysical journal},
      volume       = {102},
      number       = {2},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-23113},
      pages        = {351 - 359},
      year         = {2012},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The 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.},
      keywords     = {Animals / Apoproteins: chemistry / Entropy / Heme:
                      chemistry / Horses / Molecular Dynamics Simulation /
                      Myoglobin: chemistry / Neutron Diffraction / Protein
                      Stability / Protein Unfolding / Time Factors / Transition
                      Temperature / Apoproteins (NLM Chemicals) / Myoglobin (NLM
                      Chemicals) / Heme (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-1 / JCNS-1 / ICS-5},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)ICS-5-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung (FUEK505) / 544 - In-house Research
                      with PNI (POF2-544)},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-HGF)POF2-544},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22339872},
      pmc          = {pmc:PMC3260689},
      UT           = {WOS:000299244100021},
      doi          = {10.1016/j.bpj.2011.12.031},
      url          = {https://juser.fz-juelich.de/record/23113},
}