Showing posts with label Biodesign. Show all posts
Showing posts with label Biodesign. Show all posts

Updates...




Just felt the need to report whats been happening this week.

Monday I attended ST3's Bella Doll Casting Call at the Crown Room.

It was a good night, with VJ steel on the decks.
For the full gallery at 944, courtesy of photographer Joseph Greenbaum click here



Monday, I was also informed that I had been selected for a job. So at least I will be keeping busy over the break.


Wednesday, marked the last day of the semester for me. All of my final exams went smoothly and I am now just waiting for my grades to come through. I am however, taking a medical anthropology class over the winter break.


Last night, I attended the second of my volunteer training sessions at Phoenix Childrens Hospital. It was all pretty self explanatory stuff, yet I did learn how to properly remove personal protective equipment, change a diaper and the correct way to hold a baby.

So for now I can rest for a few days and attempt to enjoy the holidays.

Self-destructing bacteria improve renewable biofuel production

TEMPE, Ariz.- An Arizona State University research team has developed a process that removes a key obstacle to producing lower-cost, renewable biofuels. The team has programmed a photosynthetic microbe to self-destruct, making the recovery of high-energy fats--and their biofuel byproducts--easier and potentially less costly.

read more at biodesign

Pulling single biomolecules apart: Observations and Theory

Biological Physics Seminar - Fall 2009

"Pulling single biomolecules apart: Observations and Theory"


Olga Dudko

Univ. of California at San Diego
Date: Wednesday, December 2, 2009
Location: Biodesign B105
Time: 4:00 - 5:00 pm
Host: Robert Ros
Abstract
Recent advances in biophysical techniques enable experimentalists to exert forces on individual molecules and observe their response in real time. With the spectacular resolution of piconewton forces and sub-nanometer distances, single-molecule manipulation experiments reveal details that are typically lost to ensemble averaging when studied by traditional \"bulk\" methods. However, interpretation of the experimental observables in terms of the underlying molecular interactions and structures is a challenging task. I will present a theory of single-molecule force spectroscopy, and illustrate the use of the theory by analyzing the nanopore unzipping of individual DNA hairpins, unfolding of single protein molecules with an atomic force microscope, and other experiments.

ASU Biodesign + 'Personalized' Medicine



ASU Spotlight, Ep. 102: The ASU Biodesign Institute is working on making medicine more 'personalized'.

Hydration and bulk solvent fluctuations drive protein fluctuations

Biological Physics Seminar - Fall 2009

"Hydration and bulk solvent fluctuations drive protein fluctuations"
Robert Young
Northern Arizona University
Date: Wednesday, November 18, 2009
Location: Biodesign B105
Time: 4:00 - 5:00 pm
Host: Dmitry Matyushov
Abstract
Proteins have a hydration shell and exist in a bulk solvent. We propose distinct roles for the hydration water and the bulk solvent: 1) internal protein fluctuations are slaved to fluctuations of the hydration water; 2) large scale protein fluctuations are slaved to fluctuations of the bulk solvent. Experimental results for hydration effects on myoglobin from a broad range of tools – broadband dielectric relaxation spectroscopy, Mossbauer effect, incoherent neutron scattering, ligand binding, and transient optical spectroscopy – are given a unified explanation by our model. We extend the applications to incoherent neutron scattering data for the mean-square displacement of other hydrated protein powder samples including maltose binding protein. We have also extended the model to include effects of bulk solvent on large-scale protein fluctuations: for example, to the fluctuations of the functional cleft in dehydrated lysozyme in glycerol probed by dielectric spectroscopy, NMR, and incoherent neutron scattering. The results reinforce the concept that fluctuations of the bulk solvent drive large scale protein fluctuations. (07-13-2009. Revised 11-3-2009)
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