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Figure S1. Assumed models of force extension.
Blue dots illustrated data from the study by Fritz et al. for P-selectin/PSGL-1 ADDIN EN.CITE Fritz19986170Fritz, J.Katopodis, A. G.Kolbinger, F.Anselmetti, D.1998Force-mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopyProc Natl Acad Sci USA952112283-8Oct 139770478Base SequenceCell LineDNA PrimersHumansKineticsLigandsMembrane Glycoproteins/*chemistry/geneticsMicroscopy, Atomic ForceP-Selectin/*chemistryRecombinant Fusion Proteins/chemistrySurface Plasmon Resonancehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9770478Novartis Services AG, Scientific Services, Physics, WKL-127.620, CH-4002 Basel, Switzerland.[1]. The heavy black line illustrates the freely-jointed chain model with parameters measured by Fritz et al. ADDIN EN.CITE Fritz19986170Fritz, J.Katopodis, A. G.Kolbinger, F.Anselmetti, D.1998Force-mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopyProc Natl Acad Sci USA952112283-8Oct 139770478Base SequenceCell LineDNA PrimersHumansKineticsLigandsMembrane Glycoproteins/*chemistry/geneticsMicroscopy, Atomic ForceP-Selectin/*chemistryRecombinant Fusion Proteins/chemistrySurface Plasmon Resonancehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9770478Novartis Services AG, Scientific Services, Physics, WKL-127.620, CH-4002 Basel, Switzerland.[1]. The dashed red line illustrates the same model modified with a step superimposed at the contour measured by Fritz et al. ADDIN EN.CITE Fritz19986170Fritz, J.Katopodis, A. G.Kolbinger, F.Anselmetti, D.1998Force-mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopyProc Natl Acad Sci USA952112283-8Oct 139770478Base SequenceCell LineDNA PrimersHumansKineticsLigandsMembrane Glycoproteins/*chemistry/geneticsMicroscopy, Atomic ForceP-Selectin/*chemistryRecombinant Fusion Proteins/chemistrySurface Plasmon Resonancehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9770478Novartis Services AG, Scientific Services, Physics, WKL-127.620, CH-4002 Basel, Switzerland.[1]. The heavy green line illustrates the modified freely-jointed chain model employed in the simulation with a 92 nm contour length. The step served to simplify the model so molecular extension probabilities imposed by energetic constraints would not need to be considered in bond formation kinetics. The model still matched the data reported in the study by Fritz et al. ADDIN EN.CITE Fritz19986170Fritz, J.Katopodis, A. G.Kolbinger, F.Anselmetti, D.1998Force-mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopyProc Natl Acad Sci USA952112283-8Oct 139770478Base SequenceCell LineDNA PrimersHumansKineticsLigandsMembrane Glycoproteins/*chemistry/geneticsMicroscopy, Atomic ForceP-Selectin/*chemistryRecombinant Fusion Proteins/chemistrySurface Plasmon Resonancehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9770478Novartis Services AG, Scientific Services, Physics, WKL-127.620, CH-4002 Basel, Switzerland.[1] well. The blue dotted line illustrates the rope model. As with the modified freely-jointed chain model, bonds are unstressed until they reach their contour length. Rope bonds stretched beyond their contact length behave as a very stiff spring.
QUOTE EN.REFLIST 1. Fritz J, Katopodis AG, Kolbinger F, Anselmetti D (1998) Force-mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopy. Proc Natl Acad Sci USA 95: 12283-12288.
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