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@ARTICLE{Stacklies:94241,
      author       = {Stacklies, W. and Vega, M. C. and Wilmanns, M. and Gräter,
                      F. and DESY},
      title        = {{M}echanical {N}etwork in {T}itin {I}mmunoglobulin from
                      {F}orce {D}istribution {A}nalysis},
      journal      = {PLoS Computational Biology},
      volume       = {5},
      issn         = {1553-734X},
      address      = {San Francisco, Calif.},
      publisher    = {Public Library of Science},
      reportid     = {PHPPUBDB-12668},
      pages        = {e1000306},
      year         = {2009},
      abstract     = {The role of mechanical force in cellular processes is
                      increasingly revealed by single molecule experiments and
                      simulations of force-induced transitions in proteins. How
                      the applied force propagates within proteins determines
                      their mechanical behavior yet remains largely unknown. We
                      present a new method based on molecular dynamics simulations
                      to disclose the distribution of strain in protein
                      structures, here for the newly determined high-resolution
                      crystal structure of I27, a titin immunoglobulin (IG)
                      domain. We obtain a sparse, spatially connected, and highly
                      anisotropic mechanical network. This allows us to detect
                      load-bearing motifs composed of interstrand hydrogen bonds
                      and hydrophobic core interactions, including parts distal to
                      the site to which force was applied. The role of the force
                      distribution pattern for mechanical stability is tested by
                      in silico unfolding of I27 mutants. We then compare the
                      observed force pattern to the sparse network of coevolved
                      residues found in this family. We find a remarkable overlap,
                      suggesting the force distribution to reflect constraints for
                      the evolutionary design of mechanical resistance in the IG
                      family. The force distribution analysis provides a molecular
                      interpretation of coevolution and opens the road to the
                      study of the mechanism of signal propagation in proteins in
                      general.},
      keywords     = {Computer Simulation / Cytoskeletal Proteins: chemistry /
                      Cytoskeletal Proteins: ultrastructure / Elastic Modulus /
                      Models, Chemical / Models, Molecular / Muscle Proteins:
                      chemistry / Muscle Proteins: ultrastructure / Protein
                      Structure, Tertiary / Stress, Mechanical / Cytoskeletal
                      Proteins (NLM Chemicals) / MYOT protein, human (NLM
                      Chemicals) / Muscle Proteins (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF1-550)},
      pid          = {G:(DE-H253)POF1-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19282960},
      pmc          = {pmc:PMC2643529},
      UT           = {WOS:000266214000011},
      doi          = {10.1371/journal.pcbi.1000306},
      url          = {https://bib-pubdb1.desy.de/record/94241},
}