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Download the Protein Blotting Guide
Download the Stem Cell Guide for Life Science Researchers
Anyone familiar with scientific advances in the last few years should be well acquainted with the Personal Genome Project (PGP) launched by Dr. George Church in this 2005 Nature editorial. For those of you who have been living in a secluded cave somewhere in Afghanistan for the past 6 years, the Personal Genome Project hopes to enroll 100,000 participants from the general public who are willing to have their genomes sequenced and allow the results to be published in a massive database along with extensive information about their traits and medical history. It is hoped that the information provided will help scientists test hypotheses about the relationships among genes, traits, and environment.
Perhaps less well known is what it takes to become a volunteer for this project. In order to enroll as a volunteer, potential participants must take an entrance exam that tests basic genetics literacy, informed consent expertise, and knowledge about the rights and responsibilities of human research subjects. That’s right…you must take a test and score 100% in order to qualify for participation in the study!
In order to help volunteers study for this exam, the Alan and Priscilla Oppenheimer Foundation have created a Personal Genome Project Study Guide which has information on:
genetic material
gene transmission
gene expression
gene regulation
genetics and society
project literacy
We thought that it would be fun for readers of this blog, who should be more familiar with the above topics than the average PGP volunteer, to take the practice tests associated with the study guide to see how much they actually remember from their first year courses! The tests are multiple choice so that should help prevent total embarrassment, but my guess is that most of us would not score 100% without preparing in advance. I took the gene transmission test and scored 9/10. Not enough to qualify as a volunteer!
Try your hand a the tests below and let us know how well you performed. Good Luck!
I’m always on the lookout for new ways of teaching proteomics. Here’s a gem that I found on YouTube.
Directed in 1971 by Robert Alan Weiss for the Department of Chemistry of Stanford University and imprinted with the “free love” aura of the period, this short film continues to be shown in biology class today. It has since spawn a series of similar funny attempts at vulgarizing protein synthesis. Narrated by Paul Berg, 1980 Nobel prize for Chemistry.
While we are all familiar with the role of methyltransferase in DNA and protein modification in the nucleus, (think epigenetics with regards to DNA), this is the first time that methylation in the cytoplasm has been shown to promote protein complex formation.
The researchers first identified an enzyme which is mainly present in the cytoplasm and which methylates the amino acid lysine (Smyd2). Then they searched for interaction partners of the enzyme Smyd2
and found the heat shock protein Hsp90. The scientists went on to show that Smyd2 and methylated Hsp90 form a complex with the muscle protein titin.
According to the authors, “Titin is the largest protein in the human body and known primarily for its role as an elastic spring in muscle cells. Precisely this elastic region of titin is protected by the association with methylated Hsp90.”
In skeletal muscle cells of the zebrafish, the team explored what happens when the protection by the methylated heat shock protein is repressed. By genetic manipulation they altered the organism in such a way that it no longer produced the enzyme Smyd2, which blocked the methylation of Hsp90. Without methylated Hsp90, the elastic titin region was unstable and muscle function strongly impaired; the regular muscle structure was partially disrupted.
Click here for a link to the Genes and Development paper.
In what I feel might be the most important piece of journalism published last week, the LA Times reported that scientists have uncovered the compound that is responsible for lowering the risk of type two diabetes in coffee drinkers.
According to a study published in the Journal of Agricultural and Food Chemistry, Coffee Components Inhibit Amyloid Formation of Human Islet Amyloid Polypeptide (hIAPP), a documented causative factors of type 2 diabetes.
Why you’ll never find a Muppet with type 2 diabetes:
Apparently, the editors at the Times may have been a few cups behind themselves since the original paper was published in November of last year. Nonetheless, with this kind of news, it is better to hear it late than never.
I just hope that the authors were diligent with their research methods and not dishonest like the UConn scientist who published fraudulent data bolstering the beneficial effects of resveratrol which is found in red wine and has allegedly been linked to improved cardiac health. It has taken me many difficult mornings to recover from that report and I have become quite depressed realizing that my morning after hangovers were for naught. Indeed, my only consulation has come from knowing that the coffee I have consumed to counter the negative effects of drinking too many cups or red wine, (all for their cardioprotective effects of course), wil go a long way to protecting me from acquiring type 2 diabetes.
Citation
J. Agric. Food Chem., 2011, 59 (24), pp 13147–13155, Publication Date (Web): November 7, 2011 (Article), DOI: 10.1021/jf201702h
So you’ve isolated your protein, ran them on a gel and now you’re ready to transfer them to a membrane to begin western blotting. Sounds simple, right? Not so fast. Don’t forget to equilibrate your gel prior to beginning your transfer. Gel equilibration generally involves rinsing the gel in diH2O and soaking it in transfer buffer for approximately 15 min. While it may sound simple, (and it truly is), it is a step that might make the difference between an ugly blot and one that is publication worthy.
Below are some points to consider about gel equilibration:
Gel equilibration removes contaminating electrophoresis buffer salts. If not removed, these salts increase the conductivity of the transfer buffer and the amount of heat generated during transfer.
Equilibration also allows the gel to adjust to its final size prior to electrophoretic transfer. Gels shrink or swell to various degrees in the transfer buffer depending on the acrylamide percentage and the buffer composition.
Equilibration is not necessary (i) when the same buffer is used for both electrophoresis and transfer (for example, native gel transfers), or (ii) when using rapid semi-dry transfer systems such as the Trans-Blot® Turbo™ system (consult the user manual for the system you are using).
