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Microstructure-Based Modeling Of Primary Cilia Mechanics, Nima Mostafazadeh, Andrew Resnick, Y.-N. Young, Zhangli Peng
Microstructure-Based Modeling Of Primary Cilia Mechanics, Nima Mostafazadeh, Andrew Resnick, Y.-N. Young, Zhangli Peng
Physics Faculty Publications
A primary cilium, made of nine microtubule doublets enclosed in a cilium membrane, is a mechanosensing organelle that bends under an external mechanical load and sends an intracellular signal through transmembrane proteins activated by cilium bending. The nine microtubule doublets are the main load-bearing structural component, while the transmembrane proteins on the cilium membrane are the main sensing component. No distinction was made between these two components in all existing models, where the stress calculated from the structural component (nine microtubule doublets) was used to explain the sensing location, which may be totally misleading. For the first time, we developed …
The Structure Of A Complex Of Bovine &-Thrombin And Recombinant Hirudin At 2.8-A Resolution, Jacqueline Vitali, Philip D. Martin, Michael G. Malkowski, William D. Robertson, Jerome B. Lazar, Richard C. Winant, Paul H. Johnson, Brian F.P. Edwards
The Structure Of A Complex Of Bovine &-Thrombin And Recombinant Hirudin At 2.8-A Resolution, Jacqueline Vitali, Philip D. Martin, Michael G. Malkowski, William D. Robertson, Jerome B. Lazar, Richard C. Winant, Paul H. Johnson, Brian F.P. Edwards
Physics Faculty Publications
Crystals of the complex of bovine alpha-thrombin with recombinant hirudin variant 1 have space group C222(1) with cell constants a = 59.11, b = 102.62, and c = 143.26 A. The orientation and position of the thrombin component was determined by molecular replacement and the hirudin molecule was fit in 2 magnitude of Fo - magnitude of Fc electron density maps. The structure was refined by restrained least squares and simulated annealing to R = 0.161 at 2.8-A resolution. The binding of hirudin to thrombin is generally similar to that observed in the crystals of human thrombin-hirudin. Several differences in …