TY - JOUR
T1 - Single molecule force spectroscopy data and BD- and MD simulations on the blood protein von Willebrand factor
AU - Posch, Sandra
AU - Aponte-Santamaria, Camilo
AU - Schwarzl, Richard
AU - Karner, Andreas
AU - Radtke, Matthias
AU - Gräter, Frauke
AU - Obser, Tobias
AU - König, Gesa
AU - Brehm, Maria A.
AU - Gruber, Hermann
AU - Netz, Roland
AU - Baldauf, Carsten
AU - Schneppenheim, Reinhard
AU - Tampe, Robert
AU - Hinterdorfer, Peter
N1 - Funding Information:
This study was supported by the DFG within the Research group FOR1543 : “Shear flow regulation of hemostasis – bridging the gap between nanomechanics and clinical presentation (SHENC)”, the FWF Project I 767-B11 to S.P. and P25844 to A.K., by the European Fund for Regional Development ( EFRE, Regio 13 ) and by the Klaus Tschira Foundation (to F. G.). We thank Christian Rankl (Agilent, Linz) for his support in data evaluation, as well as Hermann Gruber (JKU, Linz) and Robert Tampé (Goethe-University Frankfurt) for providing cross linker. We acknowledge Sebastian Sturm and Jakob Thomas Bullerjahn for kindly providing the scripts for fitting the rupture force data at high loading rates and for helpful discussions.
Publisher Copyright:
© 2016 The Authors
Copyright:
Copyright 2019 Elsevier B.V., All rights reserved.
PY - 2016/9
Y1 - 2016/9
N2 - We here give information for a deeper understanding of single molecule force spectroscopy (SMFS) data through the example of the blood protein von Willebrand factor (VWF). It is also shown, how fitting of rupture forces versus loading rate profiles in the molecular dynamics (MD) loading-rate range can be used to demonstrate the qualitative agreement between SMFS and MD simulations. The recently developed model by Bullerjahn, Sturm, and Kroy (BSK) was used for this demonstration. Further, Brownian dynamics (BD) simulations, which can be utilized to estimate the lifetimes of intramolecular VWF interactions under physiological shear, are described. For interpretation and discussion of the methods and data presented here, we would like to directly point the reader to the related research paper, “Mutual A domain interactions in the force sensing protein von Willebrand Factor” (Posch et al., 2016) [1].
AB - We here give information for a deeper understanding of single molecule force spectroscopy (SMFS) data through the example of the blood protein von Willebrand factor (VWF). It is also shown, how fitting of rupture forces versus loading rate profiles in the molecular dynamics (MD) loading-rate range can be used to demonstrate the qualitative agreement between SMFS and MD simulations. The recently developed model by Bullerjahn, Sturm, and Kroy (BSK) was used for this demonstration. Further, Brownian dynamics (BD) simulations, which can be utilized to estimate the lifetimes of intramolecular VWF interactions under physiological shear, are described. For interpretation and discussion of the methods and data presented here, we would like to directly point the reader to the related research paper, “Mutual A domain interactions in the force sensing protein von Willebrand Factor” (Posch et al., 2016) [1].
KW - Atomic force microscopy
KW - Brownian dynamics simulation
KW - Molecular dynamics simulation
KW - Single molecule force spectroscopy
KW - von Willebrand factor
UR - http://www.scopus.com/inward/record.url?scp=85044331846&partnerID=8YFLogxK
U2 - 10.1016/j.dib.2016.07.031
DO - 10.1016/j.dib.2016.07.031
M3 - Article
VL - 8
SP - 1080
EP - 1087
JO - Data in Brief
JF - Data in Brief
ER -