Open Access. Powered by Scholars. Published by Universities.®
- Publication
- Publication Type
Articles 1 - 5 of 5
Full-Text Articles in Life Sciences
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 …
Toward The Crystallization Of An Archaeal Dihydrorotase, Haley Newman, Ryan Godin
Toward The Crystallization Of An Archaeal Dihydrorotase, Haley Newman, Ryan Godin
Undergraduate Research Posters 2018
Dihydroorotase catalyzes the conversion of N-carbamoyl-L-aspartate to Ldihydroorotate in the de novo biosynthesis of pyrimidines. M. jannaschii is an archaeon that thrives in extreme environments such as the hypothermal vents at the bottom of the oceans in which both temperature and pressure are extremely high. It can serve as a model organism for research purposes. This experiment is a first step toward elucidating the structure of this enzyme in M. jannaschii. Our summer research started using a partially purified enzyme preparation from previous experiments. We further purified the enzyme primarily using hydrophobic interaction and hydroxyapatite chromatographies. Twenty-four closely related conditions …
Purification And Crystallization Trials Of The Dihydroorotase From Methanococcus Jannaschii, Amy K. Dadisman
Purification And Crystallization Trials Of The Dihydroorotase From Methanococcus Jannaschii, Amy K. Dadisman
Undergraduate Research Posters 2017
Dihydroorotase is the enzyme that catalyzes the third step of the de novo biosynthesis of pyrimidines. M. jannaschii is a hyperthermophillic archaeon that can serve as a model organism for research purposes. This experiment is a first step toward elucidating the structure of the dihydroorotase in M. jannaschii. The enzyme was purified by salting out and heating the solution and then putting the supernatant through cation exchange chromatography and hydrophobic interaction chromatography. Twenty-four conditions were tested to determine if a crystal of dihydroorotase could be formed. Two of these conditions led to preliminary crystal formation. These findings can be utilized …
Light Scattering Study Of Elongated Particles: From Inorganic Nanorice To Polypeptide Micelles, Philip Dee
Light Scattering Study Of Elongated Particles: From Inorganic Nanorice To Polypeptide Micelles, Philip Dee
Undergraduate Research Posters 2012
Utilizing the powerful experimental technique of Dynamic Light Scattering (DLS) for size characterization of anisotropic particles can be extremely misleading. Unfortunately, this point is often not realized by researchers who strive for particle sizing of nanoparticles in suspensions. We present a consistent analysis of DDLS results on FeOOH nanorice and outline the potential difficulties and challenges of DDLS application for polypeptide micelles.
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 …