Single molecule force spectroscopy data and BD- and MD simulations on the blood protein von Willebrand factor

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• 作者：Sandra Posch^a ; ^{sandra.posch@jku.at" class="auth_mail" title="E-mail the corresponding author} ; Camilo Aponte-Santamarí ; a^b ; Richard Schwarzl^c ; Andreas Karner^d ; Matthias Radtke^c ; Frauke Grä ; ter^b ; Tobias Obser^e ; Gesa Kö ; nig^e ; Maria A. Brehm^e ; Hermann J. Gruber^a ; Roland R. Netz^c ; Carsten Baldauf^f ; Reinhard Schneppenheim^e ; Robert Tampé ; ^g ; Peter Hinterdorfer^a ; ^d ; ^{peter.hinterdorfer@jku.at" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Atomic force microscopy ; Single molecule force spectroscopy ; Molecular dynamics simulation ; Brownian dynamics simulation ; von Willebrand factor
• 刊名：Data in Brief
• 出版年：2016
• 出版时间：September 2016
• 年：2016
• 卷：8
• 期：Complete
• 页码：1080-1087
• 全文大小：1161 K

文摘

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].