I always thought that doing a speed-reading course would be a good thing to do as a scientist. With the amount of literature we need to consume, speed-reading (the art of reading faster without reducing comprehension) would save a lot of time.
But it turns out that you don’t really need to spend any cash on a course to teach you to read more quickly. There are some pretty simple steps that you can use to dramatically improve your reading speed that won’t cost you a penny.
The basic principles are:
1. Use a tracer, like a pen, or your finger, to trace under each line as you read it, as if you were underlining. You do not read text in a continuous line, but in a sequence of jumps, each of which ends with a temporary snapshot of the text within you focus area. Subconsciously, you will spend a lot of time re-reading and skipping back to previous snapshots. Using a tracer helps your eye focus and prevent this from happening.
2. Train yourself to use your peripheral vision as you read. When we read, we tend to focus just on the words that are in our central focus in each snapshot. But you can train your eye to use your peripheral vision too and so multiply your reading power.
10 minute speed-reading training
The following 10 minute training routine is based on these principles. I’ve tried it a few times recently and have seen a notable improvement in my reading speed:
1. For 2 minutes: Practice reading as fast as possible, using a tracer to guide you. Don’t worry about comprehension to begin with – that will come.
2. For 3 minutes: Train your eye to use your peripheral vision by focussing on the THIRD word and the the THIRD FROM LAST word in each line.
e.g. if the line was this, you would focus on the underlined words:
“We wish to suggest a structure for the salt of deoxyribose nucleic acid (D.N.A.).”
As you practice this and it becomes easier, you can start to move your focus into the fourth and fourth from last words and so on.
3. For 2 minutes: Practice reading each line in only two snapshots using your focus on the third and third from last words as an anchor.
4. For 3 minutes: Read too fast. Using techniques 1-3, practice reading too fast for comprehension for a couple of pages and then (still using the techniques) slow down to a pace that you can comprehend the text. This will help accustom your brain to reading more quickly — a bit like when driving a city speeds seems very slow when you have just come off the motorway.
Obviously the more you repeat the cycle, the faster you will get. If you have a go, please drop me a comment – I’d be interested to hear how it went for you.
ps: If you want to monitor your progress, measure your reading speed (words per minute) before and after. You can calculate the average number of words on a page by calculating the average number of words in 10 lines, then using this to calculate the average number of words per page and so on (but you don’t need me to tell you that!
by Nick Oswald in Organisation & Productivity
From BiteSizeBio
Monday, June 13, 2011
Sunday, June 12, 2011
Thursday, May 19, 2011
How a Jellyfish Changed Biology: the discovery and development of GFP
Fluorescent tags are widely used for microscopy and expression studies – but it wasn’t so long ago that this everyday tool was unheard of. In this article we’ll talk about how GFP came to be, and what it means for you.
Green fluoresecent protein, or GFP, was first identified in a fluorescent jellyfish, Aequorea victoria. Osamu Shimomura purified GFP and described the biophysics of how it fluoresces. A few years later, Martin Chalfie reported the expression of this protein in E. coli and C. elegans. Roger Tsien is responsible for designing variants on the protein – single amino acid changes that yielded cyan, blue and yellow fluorescent proteins, and the enchanced green protein (EGFP) that is commonly used today. Shimomura, Chalfie and Tsien were awarded the Nobel Prize for Chemistry in 2008 for their work in the discovery and development of this tool. What made GFP such a game changer is the fact that it’s “auto-catalytic” – it doesn’t need any co-factors or enzyme processing to fluoresce – so it can be easily used in a wide variety of organisms.
The major applications for GFP proteins are microscopy based, since its primary value is as a visual marker for protein detection. Here are a few of the most popular ways to use GFP:
1. Translational fusion
One of the most common uses is a fusion marker, where the GFP open reading frame is cloned downstream of your favorite ORF, so that it is translated as one long protein, fusing your favorite protein to GFP. That way, wherever your protein is expressed you will see green fluoresence. This can be used in still images and is striking in images of live cells, as you can track the location and movement of proteins.
2. Transcriptional fusion
GFP can also be used in “transcriptional fusion”, where the expression of a gene and GFP are driven off the same promoter, but with an intervening stop codon. In this case, cells expressing the first gene will fill with soluble GFP – resulting in easy detection of the particular cells expressing your protein.
3. FLIP and FRAP
FRAP (fluorescence recovery after photobleaching) and FLIP (fluorescence loss in photobleaching) rely on the fact that a single GFP molecule emits fluorescent light when it’s excited, but cannot do so indefinitely. Eventually it either bleaches out or stops emitting. So, to study the dynamics of a GFP-labeled protein, you can bleach a small area of a cell and determine how long it takes fluorescently labeled protein to “leak” back into the bleached area (FRAP), or how much fluorescence decreases overall in the rest of the cell as the bleached proteins diffuse (FLIP).
4. FRET
FRET (fluorescence resonance energy transfer) is based on the different excitation and emission spectra of the different variations on GFP. In this case, two proteins are labeled with two different fluorophores, which are carefully selected so the emission spectrum of the first overlaps the excitation spectrum of the second. The cells are then imaged using a laser that excites only the first fluorophore – so the second only lights up if the two proteins are in close enough proximity that the first fluorophore sets off the second.
Check out some of the seminal papers written about GFP:
Green fluorescent protein as a marker for gene expression.
Chalfie M, Tu Y, Euskirchen G, Ward WW, Prasher DC.
Science. 1994 Feb 11;263(5148):802-5.
Wavelength mutations and posttranslational autoxidation of green fluorescent protein.
Heim R, Prasher DC, Tsien RY.
Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12501-4.
A post from bitesizebio.
Green fluoresecent protein, or GFP, was first identified in a fluorescent jellyfish, Aequorea victoria. Osamu Shimomura purified GFP and described the biophysics of how it fluoresces. A few years later, Martin Chalfie reported the expression of this protein in E. coli and C. elegans. Roger Tsien is responsible for designing variants on the protein – single amino acid changes that yielded cyan, blue and yellow fluorescent proteins, and the enchanced green protein (EGFP) that is commonly used today. Shimomura, Chalfie and Tsien were awarded the Nobel Prize for Chemistry in 2008 for their work in the discovery and development of this tool. What made GFP such a game changer is the fact that it’s “auto-catalytic” – it doesn’t need any co-factors or enzyme processing to fluoresce – so it can be easily used in a wide variety of organisms.
The major applications for GFP proteins are microscopy based, since its primary value is as a visual marker for protein detection. Here are a few of the most popular ways to use GFP:
1. Translational fusion
One of the most common uses is a fusion marker, where the GFP open reading frame is cloned downstream of your favorite ORF, so that it is translated as one long protein, fusing your favorite protein to GFP. That way, wherever your protein is expressed you will see green fluoresence. This can be used in still images and is striking in images of live cells, as you can track the location and movement of proteins.
2. Transcriptional fusion
GFP can also be used in “transcriptional fusion”, where the expression of a gene and GFP are driven off the same promoter, but with an intervening stop codon. In this case, cells expressing the first gene will fill with soluble GFP – resulting in easy detection of the particular cells expressing your protein.
3. FLIP and FRAP
FRAP (fluorescence recovery after photobleaching) and FLIP (fluorescence loss in photobleaching) rely on the fact that a single GFP molecule emits fluorescent light when it’s excited, but cannot do so indefinitely. Eventually it either bleaches out or stops emitting. So, to study the dynamics of a GFP-labeled protein, you can bleach a small area of a cell and determine how long it takes fluorescently labeled protein to “leak” back into the bleached area (FRAP), or how much fluorescence decreases overall in the rest of the cell as the bleached proteins diffuse (FLIP).
4. FRET
FRET (fluorescence resonance energy transfer) is based on the different excitation and emission spectra of the different variations on GFP. In this case, two proteins are labeled with two different fluorophores, which are carefully selected so the emission spectrum of the first overlaps the excitation spectrum of the second. The cells are then imaged using a laser that excites only the first fluorophore – so the second only lights up if the two proteins are in close enough proximity that the first fluorophore sets off the second.
Check out some of the seminal papers written about GFP:
Green fluorescent protein as a marker for gene expression.
Chalfie M, Tu Y, Euskirchen G, Ward WW, Prasher DC.
Science. 1994 Feb 11;263(5148):802-5.
Wavelength mutations and posttranslational autoxidation of green fluorescent protein.
Heim R, Prasher DC, Tsien RY.
Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12501-4.
A post from bitesizebio.
Wednesday, May 11, 2011
Antibiotic selection is always a tool of great importance in molecular biology. But Ampicillin as an antibiotic, everyone faces a problem to some extent. The following artical is from BitesizeBio gives some helpful tips to overcome this problem.
Ampicillin is commonly used as a selection marker for plasmids in gene cloning and protein expression in E.coli and other bacteria. While it serves it’s purpose, there can be problems using this selection marker if the user is unaware of it’s limitations. This article provides a quick overview of what these limitations are and how to avoid them.
The basis of ampicillin selection is the hydrolysis and inactivation of the antibiotic by beta-lactamase expressed from the plasmid-borne bla gene. Here’s the problem: beta-lactamase is secreted by the bacteria. The resulting build-up of extracellular beta-lactamase can inactivate the ampicillin in the culture medium, removing the selective pressure, if the culture is not handled properly.
In liquid cultures, this means that a portion (possibly a very large portion) of the cells no longer have the plasmid, giving poor yielding plasmid preps, protein expression etc. On agar plates, ampicillin degradation can lead to the formation of satellite colonies on transformation plates. Satellite colonies are very small colonies of cells that have not taken up the plasmid that form around a large colony that has taken up the bla-containing plasmid. The satellites form because the beta-lactamase released by the bla-expressing colony degrades the ampicillin in the vicinity of the colony. The satellites are not necessarily a problem as they will not grow when transferred to a medium containing fresh ampicillin.
So how do you avoid plasmid loss when using ampicillin as a selection marker? Here’s how:
## Don’t allow liquid cultures to saturate for too long. I would recommend never growing cultures higher than OD600=3 (in LB)
## If you are using a starter culture, always pellet and re-suspend the starter culture in fresh, antibiotic-free medium before innoculating the main culture. This is to remove the secreted beta-lactamase from the medium.
## Use a higher ampicillin concentration if you are experiencing problems. I would recommend using 200 micrograms per mL or higher. This makes it harder for the beta-lactamase to inactivate all of the ampicillin and is especially useful for avoiding satellite formation.
## For the same reason, never use old ampicillin stocks or plates as the ampicillin will have broken down somewhat, giving a reduced effective ampicillin concentration.
If all else fails, switch to carbenicillin selection. This antibiotic is also inactivated by beta-lactamase but more slowly than ampicillin is. For this reason carbenicillin selection is far more effective than ampicillin. Unfortunately it is much more expensive!
Ampicillin is commonly used as a selection marker for plasmids in gene cloning and protein expression in E.coli and other bacteria. While it serves it’s purpose, there can be problems using this selection marker if the user is unaware of it’s limitations. This article provides a quick overview of what these limitations are and how to avoid them.
The basis of ampicillin selection is the hydrolysis and inactivation of the antibiotic by beta-lactamase expressed from the plasmid-borne bla gene. Here’s the problem: beta-lactamase is secreted by the bacteria. The resulting build-up of extracellular beta-lactamase can inactivate the ampicillin in the culture medium, removing the selective pressure, if the culture is not handled properly.
In liquid cultures, this means that a portion (possibly a very large portion) of the cells no longer have the plasmid, giving poor yielding plasmid preps, protein expression etc. On agar plates, ampicillin degradation can lead to the formation of satellite colonies on transformation plates. Satellite colonies are very small colonies of cells that have not taken up the plasmid that form around a large colony that has taken up the bla-containing plasmid. The satellites form because the beta-lactamase released by the bla-expressing colony degrades the ampicillin in the vicinity of the colony. The satellites are not necessarily a problem as they will not grow when transferred to a medium containing fresh ampicillin.
So how do you avoid plasmid loss when using ampicillin as a selection marker? Here’s how:
## Don’t allow liquid cultures to saturate for too long. I would recommend never growing cultures higher than OD600=3 (in LB)
## If you are using a starter culture, always pellet and re-suspend the starter culture in fresh, antibiotic-free medium before innoculating the main culture. This is to remove the secreted beta-lactamase from the medium.
## Use a higher ampicillin concentration if you are experiencing problems. I would recommend using 200 micrograms per mL or higher. This makes it harder for the beta-lactamase to inactivate all of the ampicillin and is especially useful for avoiding satellite formation.
## For the same reason, never use old ampicillin stocks or plates as the ampicillin will have broken down somewhat, giving a reduced effective ampicillin concentration.
If all else fails, switch to carbenicillin selection. This antibiotic is also inactivated by beta-lactamase but more slowly than ampicillin is. For this reason carbenicillin selection is far more effective than ampicillin. Unfortunately it is much more expensive!
Wednesday, April 27, 2011
Monday, March 28, 2011
Wednesday, February 16, 2011
Coca Cola Original recipe
Coca Cola is popular drink for so many years ... but its recipe was kept secret. The only written known is stored in a volt at atlanta. But recently a very old photograph is published which shows the secret recipe of Coca Cola.
Want to try at home?
Want to try at home?
Tuesday, February 15, 2011
Friday, February 11, 2011
Eat Bread !!!!!!!!!
Kittiwat Unarrom, a talented artist from Thailand, uses his skills to create unique loafs of bread shaped like various human body parts.
Kittiwat has experimented with many art forms, from painting to sculpting, but it wasn't until he had to return home and take over the family bakery that he discovered his true passion - making grotesque-looking bread. Since he first started out, in 2006, he has made a name for himself, and his Body Bakery has become a popular tourist attraction.
The gruesome bread Kittiwat Unarrom makes is incredibly realistic looking, but to achieve this level the artist spent many hours studying human anatomy and visiting forensic museums. At the same time, he found it important to make his bread delicious as well, because he didn't want his art to be just an object of art, he wanted audiences to feel involved. His first batch was pretty good, but it wasn't delicious, so he kept improving the recipe until he got the taste just right.
When he first started working at his family's bakery, he was convinced he wasn't going to get to practice his art anymore, but as soon as he discovered dough, he realized the possibilities are endless. Every day he works with the dough he gets new ideas about new edible art projects, and he believes art shouldn't be limited to art galleries and museums.
His body-part bread looks just like the real thing, but he admits it's pretty strange eating someone's head, piece by piece, and looking in their eyes at the same time. In case you were thinking of going to Thailand for a piece of human-looking bread, forget about it, Kittiwat's bakery is only selling normal bread, at least for the moment.
From: Fropki.
Kittiwat has experimented with many art forms, from painting to sculpting, but it wasn't until he had to return home and take over the family bakery that he discovered his true passion - making grotesque-looking bread. Since he first started out, in 2006, he has made a name for himself, and his Body Bakery has become a popular tourist attraction.
The gruesome bread Kittiwat Unarrom makes is incredibly realistic looking, but to achieve this level the artist spent many hours studying human anatomy and visiting forensic museums. At the same time, he found it important to make his bread delicious as well, because he didn't want his art to be just an object of art, he wanted audiences to feel involved. His first batch was pretty good, but it wasn't delicious, so he kept improving the recipe until he got the taste just right.
When he first started working at his family's bakery, he was convinced he wasn't going to get to practice his art anymore, but as soon as he discovered dough, he realized the possibilities are endless. Every day he works with the dough he gets new ideas about new edible art projects, and he believes art shouldn't be limited to art galleries and museums.
His body-part bread looks just like the real thing, but he admits it's pretty strange eating someone's head, piece by piece, and looking in their eyes at the same time. In case you were thinking of going to Thailand for a piece of human-looking bread, forget about it, Kittiwat's bakery is only selling normal bread, at least for the moment.
From: Fropki.
My wedding : second session
My actual wedding took place on January 7 2011. After that staying a week there I came to LosBanos to my work place. I was invited for a simple dinner to some of my friends here. To my surprise they arranged a crazy program. That was something I will remember throughout my life. Thank you guys for the nice evening.
Here are the videos of that event.
Part 1
Part 2
Thanks Andy, Aryo, CJ, Park, Manish, Diago and also Jasmin :)
Here are the videos of that event.
Part 1
Part 2
Thanks Andy, Aryo, CJ, Park, Manish, Diago and also Jasmin :)
Thursday, February 10, 2011
Friday, February 4, 2011
Thursday, February 3, 2011
Subscribe to:
Posts (Atom)